Biochemistry

Biochemistry Final (Eng Version)
Task №1
In some diseases, the patient's body temperature rises, which is
considered as a protective reaction of the body. However, high
temperatures are destructive to the body's proteins. Explain why
when the temperature is above +40° C, the function of proteins is
disturbed and there is a threat to human life.
Algorithm of the decision:

1. The structure of proteins and bonds that hold their structures
in the native conformation.
2. How does the structure and function of proteins change with
temperature increase?
3. What is the optimum temperature for an enzyme? Reversible
and irreversible inactivation.
Heat (high temperature) causes protein denaturation, which

results from disruption of non-covalent bonds, which are
responsible for stabilizing structural organization of protein
molecule. Ionic and hydrogen bonds are the most weak and when
the temperature of the molecules increases, the kinetic energy
also increases causing the molecules to vibrate so rapidly and
violently, so that the weaker hydrogen and ionic bonds break
unravelling (denaturing) the protein to its primary (inactive)
structure.
Since the cells and enzymes of the human and animals
organism consist mostly of proteins, the influence of high
temperature can lead to the irreversible denaturation which can
cause the disorders of biochemical processes or even the death.
1. Primary structure describes the unique order in which amino
acids are linked together to form a protein. Proteins are
constructed from a set of 20 amino acids. All amino acids have the
alpha carbon bonded to a hydrogen atom, carboxyl group, and an
amino group. The "R" group varies among amino acids and
determines the differences between these protein monomers.
Bond type: Peptide bond
Secondary structure refers to the coiling or folding of a polypeptide
chain that gives the protein its 3D shape. There are two types of
secondary structures observed in proteins. One type is the alpha
(α) helix structure. This structure resembles a coiled spring and is
secured by hydrogen bonding in the polypeptide chain. The
second type of secondary structure in proteins is the beta (β)
pleated sheet. This structure appears to be folded or pleated and
is held together by hydrogen bonding between polypeptide units of
the folded chain that lie adjacent to one another.
Bond type: Hydrogen bond
Tertiary structure
The general form or conformation (3D structure) of the polypeptide
chain. The polypeptide chain is laid to form a dense structure. Two
forms of tertiary structure are possible - globular and fibrillar.
Shrinkage of the protein into the tertiary structure makes the
protein molecule 10 times more compact than the original
polypeptide chain. In the tertiary structure, proteins consisting of
one polypeptide chain acquire biological activity. The tertiary
structure is the highest structure for molecules with a single
polypeptide chain.
Bond type: Disulfide bridge, ionic binding, hydrophobic
interactions.
Quaternary structure refers to the structure of a protein
macromolecule formed by interactions between multiple
polypeptide chains. Each polypeptide chain is referred to as a
subunit. Proteins with quaternary structure may consist of more
than one of the same type of protein subunit. They may also be
composed of different subunits. Hemoglobin is an example of a
protein with quaternary structure. It contains four subunits: two
alpha subunits and two beta subunits.
Bond type: Disulfide bridge, ionic binding, hydrogen bond.
2. The increase in temperature causes the protein denaturation,
which results in the unfolding and disorganization of a
protein’s secondary and tertiary structures without the
hydrolysis of peptide bonds. Denaturation may, under ideal
conditions, be reversible, such that the protein refolds into its
original native structure when the temperature is decreased.
However, most proteins, once denatured, remain
permanently disordered. Denatured proteins are often
insoluble and precipitate from solution.
3. Almost all enzymes are thermolabile. The reaction rate
increases about 2 times with increasing temperature for
every 10° C, this ratio is maintained up to a certain
temperature (37°-45° С), a further increase will cause a
slowdown in the reaction rate. This is determined by the
protein nature of the enzymes, as the temperature above 60°
С and above causes irreversible protein denaturation.
The temperature at which enzymes have maximum activity is
called the temperature optimum. When the temperature drops
below the optimum or the temperature rises above 40° C, the
enzymes show inactivation.
There are reversible and irreversible inactivation. With reversible
inactivation, the enzyme is able to restore its activity if it is again in
the optimum temperature mode. This is observed when the
temperature drops.
0-60° C - reversible denaturation,

above 60° - irreversible denaturation.
Task №2
In the patient's urine with phenylketonuria, phenylalanine is found -
6 mM / l (normal 0,01 mm / l) and its metabolite - phenylpyruvic
acid - 4.9 mm / l (normally absent). Why does the level of
phenylalalin in the patient’s body increase and its metabolites
appear in the urine?
1. In the absence of which enzyme, phenylalanine stops turning
into tyrosine? Write this reaction
2. Write the enzyme, the above reaction and its coenzyme,
vitamins necessary for the work of this enzyme.
3. Which recommendations should a doctor give when
identifying a newborn with phenylketonuria and how
dangerous is late diagnosis of this disease?
As a result of the mutation of the gene controlling the
synthesis of phenylalanine hydroxylase, a metabolic block
develops at the stage of conversion of phenylalanine to
tyrosine, as a result of which deamination and synthesis of
toxic derivatives, phenylpyruvic acid, become the main way
of converting phenylalanine. Inadequate synthesis of
tyrosine, which is a precursor of catecholamines and
melanin, plays a significant role in the pathogenesis of the
disease.
1. Decrease or complete absence of liver enzyme

phenylalanine-4-hydroxylase activity, which normally
catalyzes the conversion of phenylalanine to tyrosine.
2) Hydroxylase (phenylalanine)
Coenzyme: tetrahydrobiopterin (like all hydroxylases).
Vitamin B6
In the body, phenylalanine is used only in the synthesis of
proteins, the entire unused supply of amino acid is converted
to tyrosine. The enzyme phenylalanine-4-monooxygenase is
directly involved in this. The coenzyme tetrahydrobiopterin in
the reaction is oxidized to dihydrofomy.
3) The main way to treat phenylketonuria is (completely excluding
foods rich in protein and phenylalanine: meat, fish, cheese, cottage
cheese, eggs, legumes, etc. Considering the duration and
complete elimination of phenylalanine from food, the splitting of its
own proteins becomes possible, which leads to the depletion of the
patient's body. For this reason, the need for protein is offset by
amino acid mixtures and protein hydrolysates. After 6 months of
age, the symptoms of phenylketonuria become more pronounced:
mental retardation; slow growth; reducing the size of the skull; the
child later begins to sit and walk; late teething; a peculiar gait:
small steps, wiggle, lowered neck and head, legs wide apart and
bent at the hip joints; a kind of posture while sitting: legs all the
time tense, due to muscle tone; possible epileptic seizures;
dermophragism and pronounced cyanosis of the extremities;
intolerance to sunlight; high sensitivity to injury; excessive
sweating and a characteristic "mouse" smell; dermatitis, severe
eczema; constipation.
Task №3
A 35-year-old patient came to the clinic with complaints of
inflammatory processes oral mucosa, muscular fatigue,
conjunctivitis. The patient ate for a long time monotonously,
eliminating from her diet products such as liver, rye, milk, yeast.
The doctor diagnosed hypovitaminosis B2. Explain the causes of
the observed symptoms.
1) Name the coenzymes that include this vitamin and their
structure, show
schematically.
2) Give examples of enzymes with these coenzymes.
3) Indicate in which reactions these enzymes are involved (write
one of them).
Riboflavin is a component of FMN and FAD. There are 2 types of
chemical reactions: 1) the enzyme performs direct oxidation with
the participation of oxygen, i.e. dehydrogenation of the original
substrate or intermediate metabolite, 2) transfer of electrons and
protons from reduced pyridine coenzymes. Enzymes of this group
play a major role in biological oxidation. In the catalytic cycle, the
isoalloxazine residue of FAD or FMN undergoes a reversible
reduction with the addition of electrons and hydrogen atoms to N1
and N10. FMN and FAD bind strongly to the protein component.
There is a direct link between the degree of riboflavin deficiency in
animals and the accumulation of lipid peroxidation products (LPO)
in the blood, the development of atherosclerosis and cataracts.
These disorders indicate the important role of flavoproteins in the
molecular mechanisms of the synthesis and decomposition of LPO
products.
The use of this vitamin protects the eyes from overwork,
neutralizes the adverse effects of ultraviolet rays on the retina, and
also prevents the occurrence of cataracts and other problems.
Vitamin B2 is able to provide ATP synthesis and the correct course
of important redox processes, the organs of the cardiovascular
system can receive the necessary energy.
Vitamin B2 is able to effectively transform all fats and
carbohydrates into energy. Riboflavin helps to evenly distribute
protein throughout muscle tissue, as a result of which muscles
begin to grow faster and more efficiently.
1) In the intestinal mucosa after the absorption of vitamin occurs
coenzymes FMN (flavin mononucleotide) and FAD (flavin adenine
dinucleotide)
2) FAD and FMN coenzymes are part of the flavin enzymes that
take
participation in redox reactions.
The main sources of riboflavin are liver, kidney, chicken yolk
eggs, cottage cheese: Vitamin contains more vitamin in sour milk
than fresh.
Task №4
After long-term treatment with anti-TB drugs (tubazid, ftivazid), the
patient developed increased irritability, sometimes convulsions,
dermatitis, and frequent stomatitis. Biochemical analysis of blood
showed the presence of hypochromic anemia,
hyperaminoacidemia, in the urine a lot of oxalates and amino
acids, especially homocysteine and cystathione. Explain the
mechanism of the listed symptoms.
1) Specify the chemical and biological name of the necessary
vitamin in this case and its letter designation.
2) Name the vitamers of this vitamin.
3) Give examples of reactions accelerated by the enzymes that
make up this vitamin.
With a lack of vitamin B6, there are numerous disorders in
metabolism, especially in the metabolism of amino acids -
hyperaminoacidimia and aminoaciduria develop. Oxalouria is
noted, caused by a disturbance of glyoxalic acid metabolism and a
negative nitrogenous balance. In addition, homocystienuria and
cystathioninuria are observed, as well as a violation of tryptophan
metabolism. Synthesis of vitamin PP from tryptophan, heme
synthesis (hypochromic anemia), and protein are impaired.
Violation of protein synthesis is accompanied by anemia and
leukopenia. Stomatitis, glossitis develops, central nervous system
excitability increases up to convulsions, polyneuritis. The
development of seizures is associated with the involvement of the
vitamin in the formation of GABA - the inhibitory mediator. With a
vitamin deficiency, glutamate is not decarboxylated and GABA is
not formed. The lesion of the skin and mucous membranes is
associated with a deficiency of vitamin PP, which is the case with
vitamin B6 hypovitaminosis.
In adults, hypovitaminosis B6 is observed with long-term treatment
of tuberculosis with isoniazid.
1. Water-soluble, Vitamin B6, pyridoxine, antidermatitic , daily
need 2-4 mg.
2. Vitamin B6 has 3 vitameres: pyridoxine or pyridoxol,
pyridoxal, pyridoxamine.
3.
Task №5
Residents of South America, where maize predominates in the
diet, often suffer from a disease for which the main symptoms are
damage to the nervous system (dementia), damage to the
digestive system (diarrhea), and symmetrical lesion of exposed
skin (dermatitis). Explain the mechanism of the listed symptoms.
1) Indicate the chemical and biological name of the necessary
vitamin in this case and its letter designation
2) What is the name of this vitamin antivitamin; what products does
it contain and what is its mechanism of action
3) From which amino acid in the body this vitamin can be formed,
write its formula. Why, in spite of the fact that this vitamin can be
formed in the body from one of the amino acids (to name it), does
avitaminosis develop when stopping the ingestion of the vitamin in
the body with food?
1) Water-soluble vitamin PP, nicotinamide, antipellagric, daily
requirement of 15-25 mg (vitamin deficiency).
Avitaminosis. Vitamin PP deficiency leads to a disease of
pellagra which is characterized by three main features:
dermatitis, diarrhea, dementia. When pellagra first develops
inflammation of the mucous membranes of the mouth
(stomatitis), tongue (glossitis), esophagitis, erosion and ulcers of
the gastric mucosa, enteritis and colitis, which is accompanied
by diarrhea. Diarrhea is caused by atrophy of the gastric and
intestinal mucosa.
Then, symmetrical skin lesions appear in open areas - neck,
cheeks, hands. Initially, redness, then swelling, darkening with
further desquamation. Dermatitis is developing. The damage of
mucous membranes and skin is based on the violation of DNA
ligase activity, this explains that the damaged cells are not
restored. Dementia is the result of chronic recurrent CNS
damage. weakening of memory is observed, then deeper
disturbances of the central and peripheral nervous systems
occur - memory loss, hallucinations, delusions, mental changes,
and severe headaches.
2) Pyridine sulfonic acid, found in corn. Compounds that in some
way specifically inactivate a vitamin, for example, by modifying it,
or limiting biological activity.
Isoniazid - violates the formation of pyridoxal phosphate coenzyme

necessary for the synthesis of amino acids.
3) Nicotinamide can be formed from tryptophan (out of 60
tryptophan molecules 1 nicotinamide molecule can be formed)
in the intestine (bacteria) and in cells in the presence of vitamin
B6.
tryptophan
Nicotinamide can be formed from tryptophan, which is an

essential amino acid, not synthesized in the body, and therefore
must necessarily come from food.
Task №6
В A child living in the North, where insolation is reduced, received
fish oil for the prevention of rickets. On examination, the early
ossification of the skull and the deformation of the skeleton due to
the slow growth of bones in length were found. Mother's
complaints of constipation in a child, weight loss, poor appetite.
Explain the cause of the child’s condition.
Hypervitaminosis D or excessive intake of vitamin D, which leads
to intoxication. There may be constipation, hypertension, muscle
rigidity. In children, happens early
ossification of the fontanelles, (роднички ) which adversely affects
on mental development.
1.What kind of exchange is impaired in a child. What is the name

of the vitamin?
2.Show the scheme of the formation of vitamin in the skin and its
further metabolism in the liver and kidneys.
3.Show the mechanism of action of this vitamin and its metabolic
forms on the intestinal wall.
1) Due to hypervitaminosis, an earlier ossification of the skull

occurs, which effects on mental activity. The calcium content in
the blood rises, resulting in calcification of the internal organs.
Characterized by decreased appetite, constipation, weight loss,
dehydration. Phosphorus-calcium metabolism is impaired.
Vitamin D - derivative of cyclopentanpergidrofenanthrene, has 9
vitamers, most active for human are D2- Ergocalciferol and D3-
cholecalciferol.
2) . Vitamin D is formed from sterols during their ultraviolet

irradiation, therefore it is called the vitamin of sunlight. Vitamin D2
is formed by ultraviolet irradiation from ergosterol, vitamin D3, 80%
is produced in the skin by UV irradiation from 7-
dehydrocholesterol.
Ergocalciferol and cholecalciferol in the liver, by oxidation, form 25-

hydroxy-ergocalciferol and 25-hydroxycholecalciferol, which are
transported with blood as part of a special calciferol-binding protein
to the kidneys, where further oxidation takes place, and 1,25-
hydroxycalciferol are formed in the kidneys, which are one of the
most active forms of vitamin.
3) Vitamin D maintains the level of inorganic phosphorus and

calcium in the plasma above the threshold value and increases
calcium absorption in the small intestine, thus preventing the
development of rickets and osteomalacia. In the intestinal mucosa
under the action of metabolic-active forms of vitamin D increases
the synthesis of calcium-carrying protein. Calcium-carrying protein
facilitates the transfer of calcium into the blood. The kidney
increases the synthesis of calcium-carrying protein, which
increases the reabsorption of calcium, as well as sodium,
phosphorus, amino acids and citrate.
 Distribution in nature.
The greatest amount of vitamin D is found in products of
animal
origin: butter, yolk of eggs, fish oil.
Prophylactic dose of Vitamin for pregnant women and
children : in the autumn-winter period and in the North is
equal to - 0.025-0.05mg/day.
Task №7
A patient suffering from cirrhosis of the liver after prolonged
alcohol abuse, with an unbalanced diet dominated by
carbohydrates, complains of heart pain, numbness of the fingers,
pain in the calf muscles, poor memory. A blood test showed the
presence of acidosis by increasing the concentration of pyruvate
and lactate. Explain the mechanism of these signs.
Patient has lack of vitamin B1, and due to this, his disease is
Polyneuritis.
All the symptoms mentioned above, because of the several stages
of Polyneuritis.
Numbness of the fingers :polyneuritis is characterized by
degenerative nerve modification. (изменения в нервах)
First of all pain in nerve trunk(ствол нервов ) increases, then
losing of skin sensitivity. Those changes connected with the
violation of synthesis of enzymes, containing B1.
Pain in muscles : In polyneuritis Pyruvate accumulates,
(накапливается )
which in anaerobic conditions is restored to lactic acid (lactate).
Lactate causes
low pH and muscle pain.
Poor memory : The second most important symptom of the
disease
the occurrence of Wernicke-Korsakov's (название
энцефалопатии ) encephalopathy,
which is characterized by memory loss, a decrease
intelligence, mental disorder
(hallucinations, fears, irritability).
Heart pain : In severe form of deficiency of thiamine (B1) , it
causes
destruction of the cardiac activity, which characterized by violation
of the heart rhythm and in appearance of pain in the heart. WHY?
BECAUSE : It turned out that a-ketoglutarate turns into y-
oxykeglutaric acid, which has a cardiotoxic effect.
Algorithm of the decision :

1) What kind of exchange is abnormal in a patient? What is the
name of the vitamin?
2) Write the reaction that produces pyruvate and lactate in this
case. Name enzymes, coenzymes, vitamins in their composition
3) Write the reaction that pyruvate undergoes under aerobic
conditions, where this reaction takes place, name the enzymes
catalyzing this reaction, indicate the coenzymes of these enzymes,
vitamins in their composition
1)Carbohydrate metabolism is impaired (aerobic decomposition of

carbohydrates), acidosis has developed, metabolic processes in
the tissues are disturbed, and cardiac activity is impaired.
Vitamin : B1 (thiamine, anti-euritic) is water-soluble, the daily
requirement is 1.5-2.0 mg.
Vitamin B1 consists from pyrimidine and thiazole rings, connected
by methine bridge. B1 becomes active after phosphorylation. In the
form of TDP (thiamine diphosphate ) it takes part in 3 enzyme
complexes: decarboxylative oxidation of pyruvate/a-ketoglutarate
dehydrogenase complex,in pentose - phosphate way of
carbohydrate conversation path.
Thiamine (B1)
2)

3)
Task №8
At the doctor’s office, the patient, in whose diet thermally
processed foods predominate, does not have fresh fruits and
vegetables in the diet. The patient complains of general weakness,
bleeding gums, loosening of the teeth, pain in the joints, poor
memory, frequent colds. On examination, numerous petechiae,
pale skin were found. A blood test showed hypochromic anemia.
Explain the mechanism of these signs.
Algorithm of decision:
1. Specify the chemical and biological name of the necessary
vitamin in this case and its letter designation
2. What foods contain this vitamin? In which enzymes does this
vitamin contain?
3. Write a reaction that is disturbed in the vitamin deficiency of
this vitamin and underlying the increased capillary fragility and
other signs of vitamin deficiency associated with connective tissue
failure; specify the enzyme.
The diagnosis of this patient is Scurvy caused by the deficiency of
Vitamin C.
Bleeding gums, loosening of the teeth, pain in the joints,
petechiae and pale skin are quite late manifestations of
hypovitaminosis C, these symptoms are present due to the
profound deficiency of vitamin C, which causes the impaired
capillary permeability due to the lack of hydroxylation of proline
and lysine in collagen, and impaired synthesis of chondroitin
sulfates.
General weakness and frequent colds are explained with the fact
that high doses of vitamin C stimulate bactericidal activity and
neutrophil migration, as well as the increase in production of
antibodies, especially Ig A and Ig M, and increase in the synthesis
of interferon, the component of the complement binding system.
This functions increases the body's need for ascorbic acid in colds
and infectious diseases.
Hypochromic anemia is present because one of the functions of
Vitamin C is the reduction of Fe3+ ion to Fe2+ ion, and promotion
of the splitting of iron from ferritin and the release of iron from the
connection with transferrin, which facilitates the absorption of iron
in the intestine, and there is an impairment of these processes
accompanied with a decrease in the synthesis of heme and
hemoglobin.
1. Biological name: Antiscorbutic or Anti-Scurvy Vitamin
Chemical name: Ascorbic Acid
Letter designation: Vitamin C
Daily need: 50-100 mg
2. The source of vitamin C is vegetable food. They are
especially rich in pepper and black currant (смородина), in
the next place are dill (укроп), parsley (петрушка), cabbage,
sorrel (щавель), citruses, wild strawberries (земляника) and
rosehips (шиповник).
Vitamin C has a well-documented participation in redox reactions
as a coenzyme of oxidoreductases in following reactions:
 hydroxylation of prolyl and lysyl residues of collagen;
 in the synthesis of hyaluronic acid and bile acids;
 in the synthesis of carnitine, necessary for the oxidation of
fatty acids;
 hydroxylation of steroids in the biosynthesis of adrenal
hormones from cholesterol;
 hydroxylation of tryptophan to 5-hydroxy-tryptophan during
serotonin biosynthesis;
 Reduction of iron ion Fe3+ to ion Fe2+ in the intestine to
improve absorption and in the blood (release from
connection with transferrin).
3. The biochemical reason for these signs is that without
vitamin C, procollagen cannot be converted to collagen,
which is the part of extracellular matrix in bones and
cartilages, as well as in the capillary walls. Collagen is
normally synthesized at the endoplasmic reticulum of a cell,
where proline and lysine residues must by hydroxylated. The
enzymes that catalyze the hydroxylation require ascorbic
acid as a coenzyme to perform their function.
Hydroxylation of proline is carried out by prolinhydroxidase with the
participation of vitamin C, Fe2+, α -ketoglutaric acid and molecular
oxygen:
OH group of hydroxyproline, forming H-O bonds between the

chains of the triplet helix of collagen, stabilizes the structure of
mature collagen;
Task №9
After prolonged treatment with antibiotics, the patient appears
frequent nosebleeds, heavy bleeding after minor cuts, retinal
hemorrhage. Reception askorutin not gave a positive effect.
Explain the mechanism of these signs.
1) Specify the chemical and biological name of the necessary
vitamin in this case and its letter designation.
2) What are the anti-vitamins and the synthetic analogue of this
vitamin called? what foods contain this vitamin.
3) Describe the biological effects of this vitamin.
The patient has low blood clotting because of this he has frequent
nose bleeds, heavy bleeding after minor cuts, retinal hemorrhage.
Reception of ascorutin did not give a positive effect as it contains
vitamin C and P. And the patient needs vitamin K
1. Vitamin K
naphthoquinone-naphthoquinone
hemostatic-antihemorrhagic
The daily need for 1.0-2.0 mg is found in green leaves of lettuce,
cabbage, spinach, nettle, as well as in some herbs (alfalfa-alfalfa,
etc.).
2. Synthetic analog-vikasol (water soluble)
Antivitamin - Dikumarol, warfarin, tromeksan.
It is found in rural clover.
3. Vitamin K1 (phylloquinone) - regulates blood coagulation in the

body, stops bleeding, accelerates wound healing.
Vitamin K is a hormonal vitamin, antioxidant vitamin and enzyme
vitamin. It has now been established that the blood coagulation
process requires the presence of at least ten active proteins. The
synthesis of five of them depends on the presence of vitamin K in
the body. Vitamin K is necessary for the liver to produce
prothrombin (a substance that promotes the formation of blood
clots), which prevents internal bleeding. In addition to procoagulant
activity, vitamin K is necessary to retain calcium in the composition
of bone tissue.
Vitamin K is also needed to build the tissues of the heart and

lungs.
Task №10
In the clinic, enzyme preparations are often prescribed for
insufficient gland
function of gastrointestinal tract and as inhibitors. What is the basis
of the
application enzymes in these cases?
1. In case of violation of the processes of digestion in the
gastrointestinal tract prescribe replacement therapy with enzyme
preparations. What enzymes are included in these drugs (indicate
the class, subclass and sub-subclass of these, enzymes, the place
of formation).
2. Show the action of enzymes involved in digestion
(schematically).
3. In acute pancreatitis (inflammation of the pancreas) prescribe
Trasilol
or other peptide trypsin inhibitors. What is the basis for the use of
inhibitors
trypsin for acute pancreatitis? (specify the type of inhibition).
1. Hydrolases enzymes catalyzing the decomposition of complex

substances into simpler ones with the participation of water.
Subclasses:
1-esterase hydrolyzing ester bonds in lipids
6 subsubclasses:
esterases of carboxylic esters (carboasterase) hydrolyze ester
bonds of TAG.
Representatives:
1)lipases( in digestive juices-gastric, pancreatic, intestinal)- speed
up
hydrolysis of lipids(TAG)
2)phospholipases- speed up hydrolysis phospholipids.There are
phospholipids A1, A2- they cleave the corresponding carboxylic
acids
and phospholipases C, D which belong to the enzymes of the II
subclass
Lipase of gastric juice-inactive and breaks down only triglycerides
enters
the stomach in emulsified form
Lipase of pancreatic juice-secreted in inactive form, activated by
salts of
bile acids.
Lipase of intestinal juice-secreted in active form,but secreted
amount of
lipase is so small that we can neglect the influence of the enzyme
phosphoesterase-hydrolyze ester bonds,formed by phosphoric
acid.Representatives: phospholipases C and d, glusoco-6-
phospatase, ATP-ase and others.
2- glycosidase hydrolyzing glycosidic bonds in carbohydrates
Representatives:α-amylase, γ-amylase, maltase, sucrase, lactase
α-amylase-breaks up starch and glucogen until maltose
maltase-breaks up maltose until 2 molecules of glucose
sucrase-breaks up sucrose until glucose and fructose
lactase-breaks up lactose until glucose and galactose
γ-amylase-breaks up glucogen until glucose
3-peptide hydrolases hydrolyzing peptide bonds in proteins and
polypeptides
2 subsubclasses:
-endopeptidases-hydrolyze peptide bonds inside molecule of
protein until
polypeptides;
Representatives:pepsin,tripsin, chymotripsin, katepsin
Pepsin secreted by cells of stomach in inactive form of pepsinogen
under
the influence of hydrochloric acid convert into pepsin;
tripsin formed in pancreatic gland in inactive form, activated under
the
influence of enteropetidases;
Chymotripsin formed in pancreatic gland in form of
chymotripsinogen
and activated by tripsin;
Katepsin is absent in digestive juices, found inside the cells,
activated in
acidic medium during inflammation and cell death;
-exopeptidases-hydrolyze peptide bonds at the ends of
polypeptides until
separate aminoacids;
representatives:
1)carboxypeptidases A and B- conjugated enzymes that contain
zinc.Formed in pancreatic gland in form of procarboxypeptidases
and activated by tripsin. They split off aminoacids from “C” end of
peptides;
2)aminopeptidases- contain in cells and intestinal juice, split off
aminoacids from “N” end of polypetide;
2. Fat digestion
Lipase:
 TAG → β-MAG + 2CFA - pancreatic lipase
 β-MAG → glycerin + СFA
 Phospholipase A1 A2:
 Phosphoglyceride → glycerin + 2CFA + H3PO4 +
nitrogenous bases
Protein digestion
Pepsin, Trypsin, Chymotripsin:
Proteins → polypeptides in the stomach and intestines
Carboxypeptidases A and B, aminopeptidases:
Polypeptides → amino acids
Carbohydrate digestion
 α-amylase:
Starch and glycogen → maltose
 Maltase:
maltose → 2glucose
 Sucrose:
sucrose → glucose + fructose
 lactase:
lactose → glucose + galactose
 γ-amylase:
glycogen → glucose
Most of the enzymes are formed in the pancreas as inactive
zymogens and only in the intestine they are converted by trypsin
into active hydrolases, premature activation is controlled by its
inhibitor, which forms a very strong complex with the enzyme.
3. Polyvalent protease inhibitor, has antiproteolytic, antifibrinolytic

and
hemostatic effect. Inactivates the most important proteases
(trypsin,
chymotrypsin, kininogenases, kallikrein, including those activating
fibrinolysis). It inhibits both the total proteolytic activity and the
activity
 of individual proteolytic enzymes.
The presence of antiprotease activity determines the effectiveness
of
lesions of the pancreas and other conditions accompanied by a
high
content of kallikrein and other proteases in plasma and tissues.
It reduces blood fibrinolytic activity, inhibits fibrinolysis and has a
hemostatic effect in coagulopathies.
Task №11
A patient admitted to the emergency room of the hospital
complained
of pain behind the sternum, burning sensation in the chest area
and poor
health. The doctor of the receiving department conducted a
biochemical
study and found: an increase in the activity of aspartate
aminotransferase
(AST). The defeat of which organ can be assumed in the patient.
The defeat of heart can be assumed in the patient.
1. Write the reaction that AST accelerates and indicate which
vitamin is
part of this enzyme
AST; coenzyme - pyridoxal phosphate B6; accelerates
transamination
reactions
2. What additional biochemical parameters should be assigned to

the patient for diagnosis?
CPK-Creatine kinase is detected in serum after 2-4 hours after
the onset of the disease. The peak is reached 24-36 hours and is
5-20 times higher than normal. CPK can be called one of the first
markers of myocardial infarction markers.
As a result of damage to the cell membrane due to hypoxia or
other causes, these intracellular enzymes enter the systemic
circulation and their activity increases. While CK-MM and CK-BB
isoforms predominate in muscle and nerve tissue, creatine kinase
MB is almost entirely in the heart muscle.
LDH1-An increase in LDH 1 and 2 is most characteristic of
damage to the heart, kidney, spleen, leukocytes, and red blood
cells, but in clinical practice it is most often used to diagnose heart
diseases, primarily myocardial infarction. The activity of total LDH
and LDH-1 increases during the first 24-48 hours after myocardial
infarction, and the maximum - on the 2-3rd day, and high speed -
within 5-10 days and can be used for late diagnosis of heart attack
In myocardial infarction: the activity of LDH-1 increases
dramatically, while the activity of LDH-2 remains stable or
increases slightly - a phenomenon called the "crossing" of LDH
isoenzymes. The intersection of LDH isoenzymes is a
characteristic symptom of myocardial infarction, and the normal
ratio of LDH-1 and LDH-2 indicates against this diagnosis.
Mioglobin- The level of myoglobin rises the very first of all
cardiac markers, the degree of increase depends on the area of
the lesion of the myocardium. This is the most "short-lived" marker
of MI - the indicator normalization occurs, as a rule, within 24
hours. This is its unique diagnostic value.
If the level of myoglobin remains elevated after an acute attack
of myocardial infarction, this is evidence of an expansion of the
infarction zone.
3. What indicator should be determined in a patient to establish

atherosclerosis?
To clarify the activity of the atherosclerotic process, standard

lipid metabolism tests are performed - total cholesterol, lipoprotein
cholesterol of very low, low and high density, triglyceride analysis,
atherosclerotic index.
Atherosclerotic index - an indicator of the prevalence of
atherosclerotic process, a pronounced relationship to the affected
and intact areas of the arteries (most often the aorta).
The probability of atherosclerosis is relatively small when the index
is less than 3.0. if the atherogenic index is in the range from 3.0 to
4.0, then the risk is regarded as moderate. If the index exceeds
4.0, the risk is assessed as high.
Task №12
Barbiturates (sodium аmital, etc.) are used in medical practice as
sleeping pills. However, an overdose of these drugs, exceeding 10
times the therapeutic dose, can lead to death. What is the basis of
the toxic effect of barbiturates on the body?
1) Draw a scheme of the process, which is influenced by these
medicines.
2) in the diagram, specify the stage of the process, which is
primarily inhibited by barbiturates.
3) Describe the consequences of their actions on the body.
1. Barbiturates affect: the transfer of electrons in the
respiratory chain and the associated phosphorylation. The
respiratory complex is a system of transmembrane proteins
and electron carriers necessary to maintain energy balance.
The balance is maintained by electron transfer.
The energy balance is a quantitative characteristic of the
production, consumption and loss of energy.
a. Scheme of the process :
Итс на русском :
Preparatory stage Oxygen-free stage
(Complex carbohydrates C6H11O5) Glycolysis (Simple carbohydrates
C6H12O6 glucose) 2 ATP excretion
Stage of complete oxygene cleavage Cell respiration (Lactic acid С3Н6О3)
СО2
36 ATP excretion
Н2О
b) Scheme of the respiratory complex (enzymatic

ensembles):
c) Electron transfer chain:

What does barbiturates do with it? !
! The work of the respiratory chain can be disturbed (and it
should not) by certain substances called specific inhibitors.
Barbiturates have properties inherent (присущим) to the
described inhibitors of the respiratory chain, (которые
спесифик) which can affect the energy reproduction during
barbiturate coma.
2) In the diagram, indicate the stage of the process that is
initially inhibited by barbiturates.
This is 1 stage of biological oxidation. Organic substances
that are intermediate products of various types of
metabolism, mainly organic acids of Citric acid cycle (CAC),
serve as the substance to be oxidized. BARBITURATES
MAY inhibit NADH2-dehydrogenase.
3) Describe the effects of their actions on the body.
Poisoning causes - narcotic intoxication, then a superficial or
deep coma, complicated by acute cardiovascular or
respiratory failure. In severe
poisoning in deep coma: breathing is rare, superficial, weak
pulse, cyanosis, narrow pupils, do not react to light, but can
expand in the terminal stage, corneal, tendon (сухожильный
) and pharyngeal reflexes are weakened or absent, diuresis
is reduced.
Task №13
A child was admitted to the clinic with diarrhea, which was
observed after feeding with milk. To make the diagnosis, a lactose
tolerance test was performed. A fasting patient was given 50 g of
lactose dissolved in water. After 30, 60 and 90 minutes the
concentration of glucose in the blood was determined. The results
showed that the concentration of glucose in the blood did not
increase. Give the possible reasons for the results, explain them.
1. Write a lactose digestion reaction scheme in the intestine,
specify the enzyme.
2. Explain why the concentration of glucose in the blood did not
increase?
3. Indicate whether this patient will experience intolerance to
fermented milk products. Explain the answer.
There are two possible options. Firstly, there may be a hereditary
deficiency of the β-glycoside complex of the enzyme lactase (a
violation of digestion), and secondly, a violation of the absorption
of monosaccharides into the enterocytes, therefore, the
concentration of glucose in the blood does not increase.
Diarrhea develops as a result of malabsorption, sugar reaching the
distal intestine alters the osmotic pressure, also after eating foods
containing milk sugar, lactose in the absence of lactase enters the
colon, where the microflora of the colon cleaves it, forming gases
(hydrogen, methane and carbon monoxide) and acids, due to this,
patients have flatulence, pain and rumbling in the abdomen,
diarrhea, feeling of fullness and bloating. The feces is liquid, light
yellow color, with a sour smell.
1. Lactose is digested by the enzyme lactase, which is located
in the enterocytes of the mucosa of small intestine.
2. Lactose is a disaccharide that is not able to be absorbed

through the walls of the small intestine, as a result of which it
must first break down into two simple sugars - glucose and
galactose. If there is hypolactasia, that is, lactase deficiency
in enterocytes of the small intestine, as a result of heredity,
therefore lactose will not be broken down into glucose and
galactose, hence the concentration of glucose has not
increased.
2. Patients with hypolactasia are required to exclude whole milk
and any products containing lactose from the diet. They are
also advised to consume milk products with removed lactose
from it.
This patient most likely will experience intolerance to fermented
milk products, because the results showed that the concentration
of glucose in the blood did not increase, he also has symptoms
such as diarrhea. Based on these signs, it is concluded that he is
prohibited to consume fermented milk products.
Nowadays, drugs containing the lactase enzyme have been
created, which are recommended for patients with pronounced
hypolactasia. These preparations, containing 250 or 500 mg of
lactase, are taken orally along with dairy food.
Task №14
Diabetes mellitus is a disease characterized by chronic
hyperglycemia (an increase in blood glucose above 6.1 mM / L on
an empty stomach), which is a consequence of insufficient
synthesis or the action of insulin. One approach to lowering blood
glucose levels is to use the drug Glucobay. Its active substance -
acarbose has the structure of tetrasaccharide and is an inhibitor of
the activity of alpha-glucosidase - enzymes of the small intestine,
involved in the digestion of carbohydrates. Explain how the
formation of glucose in the intestine and its content in the blood
during treatment with a preparation containing acarbose will
change.
Acarbose - is a hypoglycemic drug, an alpha glucosidase inhibitor
that inhibits the digestion and absorption of carbohydrates in the
small intestine and, as a result, reduces the increase in glucose
concentration in the blood after consuming carbon-containing food.
It is prescribed for ingestion in patients with insulin-dependent
diabetes mellitus in cases where a change in diet or other
hypoglycemic agents do not provide effective control over their
condition.
Glucose is normal: 3.4-6.1 mmol / l
1) Give the scheme of digestion of carbohydrates in the intestine
2) List the enzymes that are inhibited by this compound.
3) What is the type of inhibition of the activity of these enzymes
acarbose?
1) Digestion of carbohydrates
 α-amylase:
Starch and glycogen → maltose
 Maltese A:
maltose →2 glucose
 Sugar:
sucrose → glucose + fructose
 lactase:
lactose → glucose + galactose
 γ-amylase:
glycogen → glucose
2) Acarbose inhibits the enzymes (glycosidic hydrolases)

necessary for the digestion of carbohydrates, in particular, alpha-
glucosidase enzymes in the brush border of the small intestine and
pancreatic alpha-amylase. Pancreatic alpha-amylase hydrolyzes
complex starches in the lumen of the small intestine to
oligosaccharides, whereas membrane-bound intestinal alpha-
glucosidases hydrolyze oligosaccharides, trisaccharides and
disaccharides to glucose and other monosaccharides in the small
intestine. Inhibition of these enzyme systems reduces the rate of
digestion of complex carbohydrates. Glucose is absorbed in
smaller quantities because carbohydrates are not broken down
into glucose molecules.In patients with diabetes, the short-term
effect of these drugs is to lower current levels of glucose in the
blood; long-term effect is a decrease in HbA1c.
3) Competitively and reversibly inhibits pancreatic alpha-amylase
(hydrolyzes polysaccharides to oligosaccharides) and intestinal
membrane-bound alpha-glucosidases (break down oligo, tri- and
disaccharides to glucose and other monosaccharides) in the lumen
of the small intestine. Reversible inhibitors bind to the enzyme by
weak non-covalent bonds and under certain conditions are easily
separated from the enzyme. Reversible inhibitors are competitive
and noncompetitive. Competitive inhibition includes a reversible
decrease in the rate of an enzymatic reaction caused by an
inhibitor that binds to the active center of the enzyme and prevents
the formation of an enzyme-substrate complex.
Task №15
A patient has a hereditary defect of glucose-6-phosphatase in the
liver. How will glycogen metabolism change in this patient? Will
occur in this case: the synthesis of glycogen in the liver after
eating, glycogenolysis and the release of glucose into the blood in
postabsorption period?
1) Write a glycogen mobilization scheme.
2) Indicate glycogen mobilization enzymes, mark the defective
enzyme.
3) Indicate how this process differs in the liver from the process in
the muscles.
Glucose-6-phosphatase - dramatically inhibits the phosphorolytic
cleavage of glycogen, activates the enzymatic glucose transfer
with uridine diphosphoglucose by synthesizing synthesizing
glycogen, which is a substrate for further glycolytic
transformations, as well as the oxidation of glucose, including
through the pentose phosphate pathway. Finally, the splitting of
glucose-6-phosphate by phosphatase provides the flow of free
glucose into the blood, which is delivered by the blood flow to all
organs and tissues.
The disease (glycogenosis type I) manifests itself hypoglycemia,
hypertriacylglycelemia (increased blood triacylglycerol content),
hyperuricemia (increase in the content of uric acid in the blood).
Hypoglycemia occurs due to impaired formation free glucose from
glucose-6-phosphate. Besides, due to a defect of glucose-6-
phosphatase occurs accumulation of glucose-6-phosphate
substrate in liver cells, who is involved in the catabolism process
where he turns into pyruvate and lactate. The blood rises the
amount of lactate, therefore acidosis is possible. Hypoglycemia is
accompanied by a decrease in insulin and a decrease in the
insulin / glucagon ratio, which, in turn, leads to accelerated
lipolysis of adipose tissue as a result the action of glucagon and
the release of fatty acids in the blood.
Hypertriacylglycelemia results from a decrease in the activity of
lipoprotein lipase fatty tissue - an enzyme, activated by insulin and
assimilating TAG cells of adipose tissue.
Hyperuricemia results from the following processes:
- increase in the content of glucose-6-phosphate in cells and its
use in the pentose phosphate pathway to form ribose-5-phosphate
- a substrate for the synthesis of purine nucleotides;
- increase the formation of uric acid due to excess synthesis, and
therefore catabolism purine nucleotides, the end product of which
is uric acid;
- reduce uric acid excretion due to an increase lactate production
and changes in urine pH in the acidic side, which complicates the
excretion of urate - sparingly soluble salts uric acid.
1. glycogen mobilization in the liver - glycogenolysis - is the
process of glycogen breakdown to free glucose, which enters
the bloodstream. The purpose of this process is to maintain
the concentration of glucose in the blood at a constant level.
This process intensively takes place only in the liver due to
the large reserves of
glycogen.
2) Three enzymes are directly involved in glycogenolysis:

1. Phosphorylase glycogen (coenzyme pyridoxal phosphate) -
cleaves α-1,4-glycosidic bonds to form glucose-1-phosphate. The
enzyme works until 4 glucose residues remain until the branch
point (α1,6-bond).
2. α (1,4) -α (1,6) -glucantransferase is an enzyme that transfers a
fragment from three glucose residues to another chain with the
formation of a new α1,4-glycosidic bond. At the same time, one
glucose residue and an “open” accessible α1,6-glycosidic bond
remain in the same place.
3. Amylo-α1,6-glucosidase - hydrolyzes the α1,6-glycosidic bond
with the release of free (non-phosphorylated) glucose. As a result,
a chain without branches is formed, again serving as a substrate
for phosphorylase.
3)The physiological significance of glycogenolysis in the liver and
in muscles is different. Muscle glycogen is a source of glucose for
the cell itself. Liver glycogen is used primarily to maintain the
physiological concentration of glucose in the blood. The
differences are due to the presence of the enzyme glucose-6-
phosphatase in the liver cell, catalyzing the cleavage of the
phosphate group and the formation of free glucose, after which the
glucose enters the bloodstream. In the muscle cells there is no this
enzyme, and the breakdown of glycogen goes only until the
formation of glucose-6-phosphate, which is then used in the cell.
The function of muscle glycogen is that the presence of glucose-6-
phosphatase in the liver provides the main function of liver
glycogen — the release of glucose into the blood between food for
use by other organs. Thus, the mobilization of liver glycogen
ensures the maintenance of glucose in the blood at a constant
level of 3.4-6.1 mmol in the post-adsorption period. This
circumstance is a prerequisite for the work of other organs and
especially the brain.
The function of muscle glycogen is to provide cells with glucose-6-
phosphate, used in the muscle itself for oxidation and for energy or
other purposes.
Task №16
During the exam, the content of glucose in student's blood become
equal to 7mM/l. Explain the reason of those change,If student had
breakfast 4 hours before the exam.
1. Point the concentration of glucose in norm, and name the
hormone, concentration of which increases in student's blood in
these situation.
2. Write scheme of process, that activates in liver with this
hormone, and point it regulatory enzyme.
3. Describe the mechanism of action of these hormone on
regulatory enzyme and system of transmembrane transfer of
hormone signal.
1. Concentration of glucose in norm - 3.4-.6.1 mmol/l
Which hormone increases? - glucagon and adrenaline. Target
cells of adrenaline : liver, skeletal and cardiac muscles, adipose
tissue, CNS, musculate of vessels intestine, bronchus, urinary
tract.
2. Scheme of process, that activates in liver glucagon.
Regulatory enzymes :
1.Pyruvate kinase
2.Fructose 2.6 bisphosphate
Glucagon promotes the activation of phosphorylase and inhibition
of glycogen synthase. Common result of glucagon activity is -
accelerating of glucagon decay and inhibition it's synthesis in liver
(which will lead to increasing of glucose concentration. )
3. Mechanism of action of adrenaline:
Adrenaline acts by binding to a variety of adrenergic receptors.
Adrenaline is a nonselective agonist of all adrenergic receptors,
including the major subtypes α1, α2, β1, β2, and β3. Adrenaline
binding to these receptors triggers a number of metabolic changes.
Binding to α-adrenergic receptors inhibits insulin secretion by the
pancreas, stimulates glycogenolysis in the liver and muscle.
Mechanism of action of glucagon : First, cyclic AMP activates
protein kinase A, which activates phosphorylase kinase, which
phosphorylase glycogen phosphorylase b, which turns in
phosphorylase a.
Phosphorylase a is the enzyme responsible for the release of
glucose-1-phosphate, from glycogen.
Transmembrane transfer of hormone signal:
Hormones (primary mediators), by binding to receptors on the
surface of the cell membrane, form a hormone-receptor complex,
which transforms the signal of the primary mediator to a secondary
mediators. The following mediators can be secondary mediators:
cAMP, cGMP, IF3, DAT, Ca2 +, NO.
Task №17
A person performs urgent physical work (for example, runs away
from danger) 30 minutes after lunch, consisting mainly of
carbohydrates. Explain why the synthesis of glycogen stops in
skeletal muscles in this situation and stimulates its breakdown?
Because: adrenaline is a contra-insular hormone and acting on the
β2 adrenoreceptors of tissues and the liver, adrenaline brakes
glycogen synthesis in the liver and skeletal muscles.
1) Write a scheme for the synthesis of glycogen. Specify the
reactions associated with the energy spending when one glucose
molecule is included in the "seed"(затравка ) of glycogen.
2) Write a glycogenolysis scheme and specify the amount of ATP

that can be synthesized by further oxidation in the muscles of
glucose-1-phosphate till CO2 and H2O
3) Indicate which hormone levels increase in blood under stress and

how this hormone effects on the activity of regulatory enzymes of
glycogen synthesis and breakdown.
1. Glycogen synthesis
1 Mol of ATP and 1 Mol of UTP are used to incorporate one glucose
residue into the polysaccharide chain.
2. Glycogenolysis
Decay of glucagon to glucose - 6- phosphate doesn't require energy.

37-39 ATP (aerobic pathway ) and 2 ATP (anaerobic oxidative
pathway ) are formed.
3. Catecholamines - these hormones are characterized by speed

power. They are stress hormones.
Adrenaline is a catabolic hormone and affects almost to all types of
metabolism. Under his influence, tissue metabolism and glucose in
blood increases . Being a contra-insular hormone and acting on the
β2 adrenoreceptors of tissues and the liver, adrenaline enhances
gluconeogenesis and glycogenolysis, inhibits glycogen synthesis in
the liver and skeletal muscles, enhances glucose uptake and
utilization of tissues, increasing the activity of glycolytic enzymes.
Also, adrenaline enhances lipolysis (fat breakdown) and inhibits fat
synthesis. This is ensured by its effect on β1 adrenoreceptors of
adipose tissue. In high concentrations, adrenaline enhances protein
catabolism.
Task №18
Catabolism of glucose with the formation of pyruvate can occur
both in aerobic anaerobic conditions. How many ATP molecules
will be synthesized during the breakdown of glucose up to two
pyruvate molecules under aerobic and anaerobic conditions?
1. Provide a glycolysis scheme and write the reactions
associated with and ATP synthesis.
2. Write, using formulas, the oxidative glycolysis reaction.
3. Describe how NADH2 is used in aerobic and anaerobic
conditions.
Forms 37-38 ATP (aerobic pathway) and 3 ATP (anaerobic
oxidation pathway)
2)
1)
3) NADH2 under anaerobic conditions goes for the addition of
hydrogen to acetaldehyde or pyruvate, under aerobic conditions in
the chain of electron transfer.
Task №19
Sprinter and stayer compete at two distances - 100 m and 10 km.
Sprinter finishes one hundred meters long, the stayer runs the
tenth kilometer. Point out the differences in energy ensuring the
work of the muscles of these runners.
1) Provide a glucose catabolism scheme that is an energy source
for work muscle of Stayer.
2) Write out the substrates involved in the dehydrogenation
reaction, specify the path hydrogen from one of the substrates to
oxygen in the BO chain (biological oxidation).
3) What are the differences in the process, in the composition of
the final products and energy effect of the specific pathway of
glucose catabolism in the Sprinter and Stayer.
Stayer: Mostly aerobic glycolysis.; the reserve of oxygen is
provided at the expense of the myoglobin connecting it; glycogen
is not very much, because 36 ATP has developed, but there are
many lipid inclusions and the activity of SDH(succinate
dehydrogenase) is high (Krebs cycle); low rate of ATP decay (due
to the activity of myosin heads).
Sprinter: An anaerobic glycolysis occurs , since it is impossible so
quickly to provide the muscles with the necessary amount of
oxygen. a lot of glycogen - a reserve of energy substrate; low
SDH activity; high rate of ATP decay, because high-intensity work.
1)Aerobic glucose oxidation involves glycolysis reactions and the
subsequent oxidation of pyruvate in the Krebs cycle and the
respiratory chain to CO2 and H2O.
2)Hydrogen atoms (protons and electrons) from an oxidizable
substrate are attached to NAD +. The reduced form of NAD +
(NADH) transfers hydrogen to flavoproteins. The fate of hydrogen
may be different. Hydrogen from flavoproteins can be transferred
directly to oxygen to form hydrogen peroxide.
3)The differences are anaerobic (2 lactate and 2 ATP) in the
Sprinter and aerobic (6 CO2, 6H2O and 36-38 ATP) in the Stayer
glycolysis.
Anaerobic:
C 6 H 12 O 6 + 2АДФ + 2 H 3 PO 4 →
→ 2 CH 3 CHOHCOOH + 2АТФ + H 2 O
Aerobic: C 6 H 12 O 6 + 2АДФ + 2 H 3 PO 4 + НАД+ →
→ 2 CH 3 CHOCOOH + 2АТФ + H 2 O + НАДН∙Н+
Task №20
Two students came to donate blood for “sugar” to the clinic. When
the test results were ready, it turned out that the first student had a
blood glucose concentration of 5.6 mm / l, and the second - 7 mm /
l. When discussing the obtained indicators, it turned out that the
second student in the morning half an hour before the examination
drank sweet tea.
Make a conclusion about the test results.
1) What caused the recommendation that the quantitative
determination of glucose in biochemical laboratories is carried out
strictly on an empty stomach?
2) What is the normal blood glucose concentration and how much
does the elevated glucose level after eating?
3) What process increases in the liver with an increase in blood
glucose after eating?
1. The first student's blood sugar is normal. The second has
physiological hyperglycemia, which is connected with the study of
blood taken in the absorptive period. Hyperglycemia is explained in
this case by the fact that sugar entered the gastrointestinal tract,
absorbed, absorbed into the blood but has not yet passed into the
cells of the body and has not undergone phosphorylation. This
analysis is recommended to do strictly on an empty stomach, since
in the case of ignorance that the patient had consumed the sweet
before, you can take the physiological norm as a pathology and
apply treatment that can harm a healthy person. Normal blood
sugar levels can be observed only in the post-adsorption period.
2. Concentration of glucose in norm - 3.4-.6.1 mmol/l
An hour or two after a meal, the rate of glucose is from 3.6 to 8
mmol / l, and then the indicator drops. If, after a few hours, the
changes did not occur, and the glycemia rates are around 7-8
mmol / l, this indicates prediabetes
3. The insulin concentration in the blood increases after a meal in
response to hyperglycemia. Normally, insulin in the liver stimulates
the formation of glycogen and inhibits glucose synthesis and
glycogen breakdown.
Task №21
Clinical manifestations of Scurvy - hemorrhages under the skin
and mucous membranes, bleeding gums, tooth loss, anemia. What
vitamin deficiency is associated with this disease and to which
process disturbance it leads?
1. Name this vitamin, write its formula.
2. Remember, in the synthesis of which protein this vitamin is
involved, describe the structure of this protein.
3. Write the reaction in which this vitamin is involved, explain its
function, name the enzyme; specify the substances necessary for
the reaction to proceed.
Scurvy is a disease caused by an acute lack of vitamin C (ascorbic
acid), which leads to impaired collagen synthesis, and the
connective tissue loses its strength.
Listed symptoms are present due to a profound deficiency of
vitamin C, which causes impaired capillary permeability due to the
lack of proline and lysine hydroxylation in collagen and impaired
chondroitin sulfate synthesis.
With this disease, hypochromic anemia is observed, since one of
the functions of vitamin C is the reduction of the Fe3+ ion to the
Fe2+ ion and stimulating the breakdown of iron from ferritin and
release iron from the connection with transferrin, which facilitates
the absorption of iron in the intestine; with a lack of vitamin C,
there is a violation of these processes, accompanied by a
decrease in the synthesis of heme and hemoglobin.
1. Vitamin C (ascorbic acid).
2. Vitamin C is involved in the process of collagen synthesis.
Collagen is a fibrillar protein with a unique structure that
forms the basis of the intercellular substance of the
connective tissue of the tendons, bone, cartilage, skin, but it
is, of course, also in other tissues.
The collagen molecule is a left-handed helix of three α-chains. This
formation is known as tropocollagen. One turn of the α-chain helix
contains three amino acid residues. In the amino acid triads, the
third amino acid is always glycine, the second is proline or lysine,
the first is any other amino acid other than the three listed.
In the matrix, collagen molecules form fibrils with tremendous
strength and practically non-stretchable. The extraordinary
properties of collagen are associated with its primary and spatial
structure.
3. In the synthesis of collagen, hydroxylation of lysine and
proline, included in the primary chain, is of paramount
importance, which proceeds with the participation of vitamin
C.
Collagen is normally synthesized at the endoplasmic reticulum of a
cell, where proline and lysine residues must by hydroxylated. The
enzymes that catalyze the hydroxylation require ascorbic acid as a
coenzyme to perform their function.
Hydroxylation of proline is carried out by prolinhydroxidase with the
participation of vitamin C, Fe2+, α -ketoglutaric acid and molecular
oxygen:
OH group of hydroxyproline, forming H-O bonds between the
chains of the triplet helix of collagen, stabilizes the structure of
mature collagen;
Task №22
After a meal containing fats and carbohydrates, the appearance of
the blood serum changes, it becomes opaque ("milk serum"), and
after 2-3 hours it looks again transparent. Explain these changes.
1) Explain why the state of the blood after ingestion of fatty foods
is described as "Alimentary hyperlipidemia".
2) Indicate which lipoproteins will prevail in serum after 1 hour after
taking a high-fat meal.
3) Specify the composition of the main components of these
lipoproteins.
1) The increase in total serum lipids is called hyperlipidemia. It is
observed after a meal - this is a physiological phenomenon
(alimentary hyperlipidemia). Lipoproteins formed in enterocytes are
immature chylomicrons. Immature chylomicrons first enter the
lymph, then the bloodstream. In the blood, immature chylomicrons
are obtained from HDL formed in the liver, apoproteins - C-II, E
and turn into mature chylomicrons. The appearance of
chylomicrons in the blood during the absorptive period makes the
blood serum opalescent. In the blood, mature chylomicrons are
exposed to the enzyme lipoprotein lipase. Lipoprotein lipase
hydrolyzes fats from chylomicrons to glycerol and free fatty acids.
ApoS-II is transferred back to HDL after removal of the TAG from
XM. Residual chylomicrons in liver cells undergo the hydrolytic
action of lysosome enzymes. Within 1-3 hours, the chylomicrons
disappear from the blood and the human serum becomes more
transparent in the post-adsorption period.
2) In the serum after 1 hour after ingestion of food saturated with
fat, XM, VLDL, LDL, HDL will prevail.
Chylomicrons (CM) are formed in intestinal cells, their function: the
transfer of exogenous fat from the intestine to the tissues (mainly
in adipose tissue), as well as the transport of exogenous
cholesterol from the intestines to the liver.
Very low density lipoproteins (VLDLs) are formed in the liver, their
role: the transport of endogenous fat synthesized in the liver from
carbohydrates to the adipose tissue.
Low-density lipoproteins (LDL) are formed in the bloodstream
from VLDL through the stage of formation of Lipoproteins of
Intermediate Density (BOP). Their role: transport of endogenous
cholesterol to the tissue.
High-density lipoproteins (HDL) are formed in the liver, the main
role is the transport of cholesterol from the tissues to the liver, that
is, the removal of cholesterol from the tissues, and then cholesterol
is excreted with bile.
Functions of chylomicrons. Delivery of dietary (exogenous) fat from
the intestines to other tissues (mainly to adipose tissue). Transport
of exogenous cholesterol from the intestines to the liver. Therefore,
chylomicrons are a transport form of exogenous fat and
exogenous cholesterol.
3)
Task №23
A 40-year-old woman found gallstones that periodically blocked
the bile duct and disrupted the flow of bile into the intestine. List all
possible effects of bile secretion.
1) Write the formulas of bile acids and explain the role of these
molecules in the digestion of fats.
2) Indicate the function of bile acids in the absorption of lipid
digestion products and draw the appropriate scheme.
3) Indicate the deficiency of which substances may occur in such
patients, and what the consequences and symptoms may be.
The sphincter shrinks arbitrarily, bile accumulates in the stomach,
and under the influence of negative factors is thrown into the
intestine and esophagus, enters the oral cavity, injuring the
delicate mucous membrane.
Such a cast causes serious complications:
• reflux gastritis - the gastric mucosa becomes inflamed, after
eating a meal, the stomach contents are re-cast into the
esophagus;
• if treatment does not begin in time, the condition is aggravated,
gastroesophageal reflux disease begins - erosive and ulcerative
lesions of the stomach and duodenum occur, the esophagus
becomes inflamed
• in the future, the functional epithelium is replaced by a cylindrical
analogue, and can make a diagnosis of Baret's esophagus. This is
the stage of the precancerous condition of the digestive organ.
 Gallstone disease is the presence of stones in the
gallbladder and bile ducts. Stones are solid formations of
various sizes from cholesterol or bilirubin. This occurs when
cholesterol (a fat-like substance) or bilirubin (a breakdown
product of hemoglobin) is present in the bile at an elevated
concentration. In this case, the other components of bile
cannot dissolve these substances. From bile, supersaturated
with them, a precipitate can form - microscopic crystals
deposited on the mucous membrane of the gallbladder. Over
time, the crystals grow and merge, gradually forming small
stones.
1. The role of bile acids:
• Participate in the emulsification of fats in the intestines

• Pancreatic lipase activators
• Included in micelles
2) Bile acids perform the following functions:
• participate in the digestion and absorption of lipids;
• are the end products of cholesterol catabolism, in the form of
which it is excreted in the feces from the body;
• are components of bile that keep cholesterol in a dissolved state
Interrelation between carbohydrate and lipid metabolism: The link
between the transition from carbohydrates to lipids is pyruvic acid
(AEC) and acetyl CoA. PVC by oxidative decarboxylation is
converted to acetyl CoA, which serves as the starting compound
for the synthesis in the body of higher fatty acids, triglycerides and
other lipids. 3-Phosphogicherinic aldehyde, arising from the
dichotomous breakdown of carbohydrates, isomerized, is
converted into phosphodioxyacetone. When the latter is restored,
phosphoglycerol is formed, which is necessary for the synthesis of
simple and complex lipids. Acetyl-CoA and glycerol - the main
products of lipid breakdown - are the starting compounds for the
synthesis of carbohydrates. Acetyl-CoA goes into PVC, and from it
into carbohydrates by reversing the reaction of their dichotomous
decomposition. The conversion of glycerol to carbohydrates goes
through 3-phosphoglyceraldehyde, and then as described above.
3) Bile acid deficiency
Cholestasis is a pathological process characterized by a decrease
or cessation of the flow of bile into the lumen of the duodenum due
to a violation of its synthesis, excretion or excretion, which may be
associated with pathological processes anywhere from
hepatocytes to duodenal papilla.
For any form of cholestasis, a number of common symptoms are
characteristic: an increase in liver size, pain and discomfort in the
right hypochondrium area, pruritus, acholic (bleached) feces, dark
urine color, and digestive disorders. A characteristic feature of
itching is its intensification in the evening and after contact with
warm water. This symptom affects the psychological comfort of
patients, causing irritability and insomnia. With an increase in the
severity of the pathological process and the level of obstruction,
the feces lose their color until complete discoloration. The stool
becomes more frequent, becoming thin and smelly. Fat-soluble
vitamins are also not absorbed, which leads to the development of
hypovitaminosis. In the cells of the intestine, most of the digestion
products are again converted to triacylglycerols. Fatty acids form
acyl-CoA, and then acyl residues are transferred to
monoacylglycerol with the participation of transacilase.
Task №24
Experimental animals received from food only glucose containing
radioactive carbon atoms. After a few hours, the fats contained in
adipocytes, and found radioactive carbon and in the composition of
glycerol and radicals
fatty acids.
Intraconversions of Carbohydrates and Lipids
1) DOAP is reduced and gives glycerophosphate that is used
on TAG and Phospholipid synthesis;
2) acetylCoA which is formed in oxidation of glucose. Then
acetylCoA can be used on synthesis of FFA, cholesterol and
ketone bodies
3) NADPH2 are formed in Pentose phosphate cycle and are
used in FFA and Cholesterol synthesis.
Lipids can be converted into carbohydrates through
phosphotrioses that are involved in gluconeogenesis.
1) Write a glucose catabolism to acetyl CoA.

Pyruvate → AcetylCoA
2) Write a scheme of liponeogenesis from phosphotriosis to
glycerol.
3) Show schematically the path of fatty acid synthesis.

Task №25
In one of the hereditary diseases in the skeletal muscles of
patients reduced the concentration of carnitine as a result of a
defect of enzymes involved in its synthesis. Why do such patients
have reduced ability to perform physical work?
Carnitine deficiency is the result of inadequate intake or inability to
absorb the amino acid carnitine. Carnitine deficiency is a
heterogeneous group of diseases. Muscle metabolism worsens,
leading to myopathy, hypoglycemia, or cardiomyopathy. Carnitine
deficiency can lead to muscle necrosis, myoglobinuria, so-called
lipid myopathy, hypoglycemia, fatty liver disease and
hyperammonemia, accompanied by muscle pain, weakness,
confusion and cardiomyopathy.
These are answers to questions 2 and 3, and yes, they need to be
written 2 times, at the beginning and at the end of the answers
themselves:
Because it is the mechanism of their work.
2) In the absence of enzymes involved in the synthesis of

carnitine, B-oxidation of FFA will be reduced. Since then all the
processes occur in the mitochondria in the absence of carnitine,
the activated fatty acid does not penetrate into the inner
mitochondrial membrane. The cells accumulate a large amount of
FLC, which are not subjected to oxidation. Patients can not
perform physical work as it does not emit ATP, which could be
formed during B-oxidation of FFA.
3) Long-chain acyl-CoA-derivatives (or FFA) cannot penetrate into
mitochondria and oxidize, if they do not previously form
acylcarnitine-derivatives. And due to the lack of carnitine, this
process of transferring FFA into mitochondria is inhibited and FLC
accumulates in the form of fat vacuoles in the cytoplasm.

1) Write a diagram showing the role of carnitine in the metabolism
of fatty acids.
2) Specify the speed of a metabolic pathway is reduced in these
patients.
3) Explain why the muscle cells of patients contain large vacuoles
of fat, visible under a microscope.
1) TRANSFER OF ACTIVATED FATTY ACIDS WITH A LONG

CHAIN THROUGH THE INNER MITOCHONDRIAL MEMBRANE
SERVES CARNITIN.
All the enzymes of B-oxidation of fatty acids are in the

mitochondria. The inner membrane is impermeable to fatty acids.
Their transfer takes place with the help of carnitine.
(CH3) 3N + -CH2-CH2-CHOH-CH2-COoH
Under the action of carnitine-acyltransferase 1, fatty acid joins the

alcohol group of carnitine.
Acyl-Scoa + Carnitine = Acylcarnitine + NScoA

2) In the absence of enzymes involved in the synthesis of
carnitine, B-oxidation of FFA will be reduced. Since then all the
processes occur in the mitochondria in the absence of carnitine,
the activated fatty acid does not penetrate into the inner
mitochondrial membrane. The cells accumulate a large amount of
FLC, which are not subjected to oxidation. Patients can not
perform physical work as it does not emit ATP, which could be
formed during B-oxidation of FFA.
3) Long-chain acyl-CoA-derivatives (or FFA) cannot penetrate into
mitochondria and oxidize, if they do not previously form
acylcarnitine-derivatives. And due to the lack of carnitine, this
process of transferring FFA into mitochondria is inhibited and FLC
accumulates in the form of fat vacuoles in the cytoplasm.
Task №26 (Aibar)
Experimental animals received an excess of glucose containing
radioactive carbon with food for 1 week. Then the animals were
hungry for 2 days. Ketone bodies containing radioactive carbon
have been found in the blood. Explain the results of the
experiments.
1) Write a glucose catabolism to acetyl CoA.
2) Show the scheme of using acetyl CoA in the synthesis of ketone
bodies.
3) What are the key enzymes of glucose catabolism and the
synthesis of ketone bodies?
1.
2)
3) Formed by the condensation of two acetyl-CoA molecules,

acetoacetyl-CoA is able to cleave coenzyme A to form free
acetoacetic acid. The process catalyzes the enzyme
acetoacetyl-CoA hydrolase (deacylase), however, this path is
not significant in the synthesis of acetoacetic acid, since the
activity of deacylase in the liver is low.
H C−CO−CH −CO−S−КоА + H O → H C−CO−CH −COOH +
3 2 2 3 2
КоА-SH.
Task №27
Two men, 60 years old, determined the level of total cholesterol
and LDL / HDL index. In both patients, total cholesterol was 6.0
mM / L, but the LDL / HDL index in the first patient was 4, and the
second was 3.1. Evaluate the data.
1) Determine which patient has a higher risk of atherosclerosis and
its complications.
2) Make a diagram showing the role of HDL in cholesterol
transport.
3) Explain why LDL is called atherogenic lipoproteins, and HDL is
antiatherogenic.
1) LDL / HDL (coefficient of atherogenicity) with its value> 3 there
is a risk of atherosclerosis, and because in the first patient it is
equal to 4, therefore, he has a higher risk.
2) HDL cholesterol is transported in the form of cholesterol esters
from the tissues to the liver. In the formation of cholesterol esters
of cholesterol in HDL plays an important role enzyme LCAT
(lecithin cholesterol acyltransferase), which catalyzes the reaction:
Cholesterol + Lecithin = Cholesteride + Lysolecithin
This reaction takes place in the hydrophilic layer of HDL, and the
resulting klesterida pass into the hydrophobic core.
HDL plays an important role in the transport of cholesterol from
peripheral tissues to the liver and in the regulation of normal
metabolism of CM and VLDL. PAPs are formed in several ways.
Immature HDL is synthesized in hepatocytes and enterocytes.
They are disk-shaped. The transformation of “disks” into spherical
particles occurs with the participation of the enzyme lecithin-
cholesterol-acyl transferase (LCAT). Under the action of LCAT, the
lecithin radical is transferred to the hydroxyl group of cholesterol,
resulting in the formation of cholesterol ester and lysolecytin.
Cholesterol esters are moved to the inner area of the bilayer disc.
During the LCAT reaction, the lipoprotein particle loses non-
esterified cholesterol and lecithin. Isolecithin, combining with
albumin, is carried away by the flow of blood. The LPAPP particle
depleted with surface lipids becomes a strong acceptor of free
cholesterol and lecithin and is constantly replenished with them. As
they become saturated with HDL cholesterol, they turn into HDL2.
Cholesterol from HDL-2 can be transferred to VLDL, which is taken
up by the liver, via the protein-cholesterol ester transfer carrier
(cholesteryl ester transferring protein, CETP). HDL cholesterol has
been shown to be the preferred substrate for bile acid formation. It
was also established that HDL is involved in the transfer of
cholesterol not only to the liver cells, but also to the cells of
steroidogenic tissues, kidneys, small intestinal epithelium, and
adipocytes.
3) HDL cholesterol transports cholesterol esters from tissues to the
liver, thereby reducing the risk of atherosclerosis. LDL transports
cholesterol from the liver to other tissues, thereby increasing the
risk of atherosclerosis.
Task №28
A high level of lactate and bile pigments are found in the patient’s
gastric juice.
Specify what diseases of the stomach are possible in this case.
1) Name the process whose product is lactate, why lactate
accumulates in
stomach and with the help of a qualitative reaction can determine
its presence?
2) Indicate the role of hydrochloric acid, the types and the normal
value of gastric acidity
juice.
3) Why bile pigments appear in the stomach, a qualitative reaction
to them.
one.
1. Lactate is formed during anaerobic glycolysis.
Lactate is found in gastric juice in gastric cancer, accompanied by
achlorhydria and delayed food evacuation. In such patients, the
gastric contents are stagnant, there is a fermentation of
carbohydrates with the formation of lactic acid.
Reaction Upelman! The method is based on the ability of lactic
acids in the presence of iron (III) phenolate to form a low-
associating iron-green lactate salt.
2. The role of SALTIC ACID:

- in the stomach, under its influence, swelling of proteins occurs,
their surface increases, which facilitates the action of gastric juice
enzymes on them
- under its action, pepsin is formed from the pepsinogen pro-
enzyme. Progestoxin is activated by pepsin.
- it has a bactericidal effect
- It contributes to the evacuation of food from the stomach,
regulating the function of the pylorus.
- it stimulates the activity of the pancreas
Types of gastric acidity:
1. The total acid is the sum of all the acid-reactive in-tv (free and
bound HCl, organics, acid phosphates) in 100 ml of gastric juice.
NORM = 40-60 TE (titration units)
2. Free HCl NORM = 20-40 TE
3. Associated HCl (with proteins). NORM = 8-12 TE
3.
Bile pigments along with bile appear in the stomach with low
acidity or in the absence of acid. In this case, the function of the
pylorus is impaired, it is relaxed, and intestinal contents can be
thrown into the stomach. This may also contribute to the loose
closure of the gatekeeper due to cicatricial processes in it.
As a result, due to bile pigments: in the presence of HCl in the
gastric juice, its color will be greenish. bilirubin is oxidized to
biliverdin. In the absence of HCl, the color of the gastric juice will
be yellow.
The reaction of PETENOKOPHERA to bile acidity! Under the
influence of sulfuric acid, sucrose is hydrolyzed, followed by the
conversion of monosaccharides to hydroxymethylfurfural.
Condensation of bile acids with hydroxymethylfurfural leads to the
formation of red substances.
Task №29
A patient with a gastric ulcer had an operation to remove a part of
the stomach. But the postoperative examination showed that the
process of protein digestion in the patient did not change
significantly. Explain the results of the survey.
1) Name peptidase, which is synthesized in the stomach, the
mechanism of its activation and activators.
2) List the pancreatic peptidases and enterocyte enzymes
(intestinal cells).
3) Name which group of peptidases these enzymes belong to.
The process of protein digestion in the patient did not change
significantly because even after surgery, the remaining part of the
gastric mucosa remained unscathed and digestion processes were
not disrupted.
1)Pepsin is an endopeptidase, that is, it cleaves the internal
peptide bonds in the molecules of proteins and peptides. It is
synthesized in the main cells of the stomach in the form of an
inactive pepsinogen proenzyme, in which the active center is
"covered" with an N-terminal fragment. In the presence of
hydrochloric acid, the conformation of pepsinogen is changed in
such a way that the active center of the enzyme is “opened”, which
cleaves the residual peptide (N-terminal fragment), i.e.
autocatalysis occurs. The result is an active pepsin that activates
other pepsinogen molecules.During the day, about 2 grams of
pepsin is synthesized.
2)Chymotrypsin is synthesized in the pancreas in the form of an
inactive precursor, chymotrypsinogen. Chymotrypsin is activated
by active trypsin and by autocatalysis. Destroys the bonds formed
by the carboxyl group of tyrosine, phenylalanine or tryptophan, or
by the large hydrophobic radicals of leucine, isoleucine, and valine.
Trypsin is synthesized in the pancreas in the form of an inactive
precursor - trypsinogen. It is activated in the intestinal cavity by the
enzyme enteropeptidase with the participation of calcium ions, and
is also capable of autocatalysis. Hydrolyzes the bonds formed by
arginine and lysine.
Elastase is synthesized in the pancreas as an inactive precursor,
proelastase. Activated in the intestinal cavity with trypsin.
Hydrolyzes peptide bosnds formed by glycine, alanine and serine.
Carboxypeptidases synthesized in the pancreas. Activated by
trypsin in the intestine. They are metalloproteins. Peptide bonds
are hydrolyzed at the C-terminus of the protein molecule. There
are 2 types: carboxypeptidase A and carboxypeptidase B.
Carboxypeptidase A cleaves amino acids with aromatic (cyclic)
radicals, and carboxypeptidase B cleaves lysine and arginine.
Aminopeptidases synthesized in the intestinal mucosa. Peptide
bonds are hydrolyzed at the N-terminus of the protein molecule.
There are 2 such enzymes: alanine amino peptidase and leucine
amino peptidase. Alanine aminopeptidase cleaves only alanine,
and leucine amino peptidase removes any N-terminal amino acids.
3)These enzymes belong to exopeptidases (aminopeptidases and
carboxypeptidase) and endopeptidases.
Task №30
A patient with suspected myocardial infarction determined the
activity of ALT (alanine aminotransferase) and AST (aspartate
aminotransferase) in the blood. Which activity of
aminotransferases will increase to a greater extent with such
pathology and why? Name other enzymes whose activity is
determined in the blood to confirm this pathology.
AST (aspartate aminotransferase) is an organotropic myocardial
enzyme. AST is an indicator of damage to the cells of the heart
muscle and liver cells.
LDH1LDH2. Lactate dehydrogenase (LDH) is one of the main
glycolysis enzymes that catalyzes the oxidation of L-lactate to
pyruvate. It is an intracellular enzyme that is present in the cells of
almost all large organs. LDH is found in the brain, kidneys, liver,
lungs, lymph nodes, myocardium, skeletal muscles, spleen, as well
as in erythrocytes, leukocytes and platelets. In myocardial
infarction, the following picture is observed: the activity of LDH-1
increases dramatically, while the activity of LDH-2 remains stable
or increases slightly - a phenomenon called the "crossing" of LDH
isoenzymes. The intersection of LDH isoenzymes is a
characteristic symptom of myocardial infarction, and the normal
ratio of LDH-1 and LDH-2 indicates against this diagnosis.

1) Write reactions that catalyze ALT and AST.
2) Explain the significance of these reactions in the metabolism of
amino acids.
3) Explain the principles of enzyme diagnostics.
1)
2) Transamination is a reversible process of transferring an amino

group from an amino acid to a keto acid to form a replaceable
amino acid. The most common source of the amino group is
glutamic acid. The enzyme catalyzing this process is
aminotransferases (transaminases), the coenzyme of which is
vitamin pyridoxal phosphate (B6).
ALT and ACT are organ-specific enzymes. In the clinic, the
determination of ALT activity is used to diagnose liver diseases
(hepatitis, jaundice), ACT activity in myocardial pathology
(myocardial infarction).
The value of transamination:
1) formation of replaceable amino acids
2) the reaction is the first stage of the indirect oxidative
deamination of amino acids
3) since the reaction is reversible, an interrelation between the
metabolism of carbohydrates and the metabolism of proteins is
possible.
3) Enzymodiagnosis consists in making a diagnosis of a disease
based on the determination of enzyme activity in human biological
fluids. The principles of enzyme diagnostics are based on the
following positions:
· When cells in the blood or other biological fluids (for example, in
the urine) are damaged, the concentration of intracellular enzymes
of the damaged cells increases;
· The amount of enzyme released is sufficient to detect it;
· The activity of enzymes in biological fluids that are detected when
cells are damaged is stable for quite a long time and is different
from normal values;
· A number of enzymes have a predominant or absolute
localization in certain organs (organ specificity);
· There are differences in the intracellular localization of a number
of enzymes
Task №31
On examination of the patient, it turned out that the concentration
of creatinine in the blood is 200 µM / L (at a rate of 88-176 µM / L).
The defeat of which body can be assumed?
1) List amino acids - precursors of creatine.
Arginine, Glycine
2) Write a scheme for the formation of creatine and indicate the
organs that are involved in this process.
Kidney stage
->bloodstream-
>>
Liver stage
->bloodstream
-->
Once in muscle, creatine is phosphorylated by ATP and forms
creatine phosphate, the enzyme creatine kinase, or creatine
phosphokinase (CFC).
3) Indicate which enzymes will increase in the blood of patients in

this case?
LDG2, creatine phosphokinase, creatine kinase
Task №32
A patient with suspected myocardial infarction determined the
activity of ALT (alanine aminotransferase) and AST (aspartate
aminotransferase) in the blood. Which activity of
aminotransferases will increase to a greater extent with such
pathology and why? Name other enzymes whose activity is
determined in the blood to confirm this pathology.
 AST (aspartate aminotransferase) is an organotropic
myocardial enzyme. AST is an indicator of damage to the
cells of the heart muscle and liver cells.
 LDH1; LDH2. Lactate dehydrogenase (LDH) is one of the
main glycolysis enzymes that catalyzes the oxidation of L-
lactate to pyruvate. It is an intracellular enzyme that is
present in the cells of almost all large organs. LDH is found
in the brain, kidneys, liver, lungs, lymph nodes, myocardium,
skeletal muscles, spleen, as well as in erythrocytes,
leukocytes and platelets. In myocardial infarction, the
following picture is observed: the activity of LDH-1 increases
dramatically, while the activity of LDH-2 remains stable or
increases slightly - a phenomenon called the "crossing" of
LDH isoenzymes. The intersection of LDH isoenzymes is a
characteristic symptom of myocardial infarction, and the
normal ratio of LDH-1 and LDH-2 indicates against this
diagnosis.

1) Write reactions that catalyze ALT and AST.
2) Explain the significance of these reactions in the
metabolism of amino acids.
3) Explain the principles of enzyme diagnostics.
1)
2) Transamination is the reversible process of transferring an
amino group from an amino acid to a keto acid to form a
replaceable amino acid. The most common source of the amino
group is glutamic acid. The enzyme catalyzing this process is
aminotransferases (transaminases), the coenzyme of which is
vitamin pyridoxal phosphate (B6).
ALT and ACT are organ-specific enzymes. In the clinic, the
determination of ALT activity is used to diagnose liver diseases
(hepatitis, jaundice), ACT activity in myocardial pathology
(myocardial infarction).
The value of transamination:
1) formation of replaceable amino acids
2) the reaction is the first stage of the indirect oxidative
deamination of amino acids
3) since the reaction is reversible, a relationship between
carbohydrate metabolism and protein metabolism is possible.
3) Enzymodiagnosis consists in making a diagnosis of a disease

based on the determination of enzyme activity in human biological
fluids. The principles of enzyme diagnostics are based on the
following positions:
When cells in the blood or other biological fluids (for example, in
the urine) are damaged, the concentration of intracellular enzymes
of the damaged cells increases;
· The amount of enzyme released is sufficient to detect it;
· The activity of enzymes in biological fluids that are detected when
cells are damaged is stable for quite a long time and is different
from normal values;
· A number of enzymes have a predominant or absolute
localization in certain organs (organ specificity);
 there are differences in the intracellular localization of a
number of enzymes
Task №33
An 18-year-old girl living in a mountain village came to an
endocrinologist with complaints of general weakness, a decrease
in body temperature, mood disorders. The patient was sent for a
blood test for TSH (Thyroid-stimulating hormone) and
iodothyronines. The results of the analysis showed an increase in
the concentration of TSH and thyroxine. What disease can be
assumed in a patient?
1. What can be the cause of such pathology and is there a link
between the place of residence and the occurrence of this
disease?
2. Scheme of regulation of the synthesis of iodothyronines.
3. What diet should be followed in order to prevent this
pathology?
In this case hypothyroidism is assumed in patient
1. The reason of such pathology is the lack of iodine intake due
to insufficient iodine content in this region.
The general weakness is explained by the fact that as a result of
insufficient formation of thyroid hormones, the synthesis of
oxidoreductases is impaired, oxidation in the tissues decreases,
and the formation of ATP decreases due to this.
During hypofunction of the thyroid gland, due to a decrease in the
number of oxidoreductases, there is not enough energy for ATP
synthesis, little energy is released as heat, which explains the
decrease in body temperature.
Mood disorders are due to the mental effect of the thyroid
hormones. Rapid changes in thyroid hormone levels, in particular,
can unsettle emotions.
2. Iodothyronines are synthesized in thyroid gland follicles, in
composition of the protein – thyroglobulin. For the synthesis
iodine is needed, daily need of which is equal to 150 mKg
1 - thyroliberin stimulates the release of TSH;
2 - TSH stimulates the synthesis and secretion of iodothyronines;
T and T - iodothyronines inhibit the synthesis and secretion of
3 4
TSH and thyroliberin.

Synthesis of iodothyronines:
1 step
st
2 step
nd
Alternative way
3. Because of the decrease in iodine intake from food, iodine-

containing drugs are prescribed to the patient. It’s
recommended to consume more seafood and iodized salt.
Task №34
The man lost consciousness. At the same time he was pale, cold
to the touch. When I tried to bring him to his senses, his
glucometer (a device for determining glucose) and a syringe fell
out of his pocket.
1) What pathological condition can be assumed and under what
disease is it observed?
-Possible after insulin administration, due to an overdose of
glucose-lowering drugs, unusual exercise, malnutrition, the level of
glucose in the blood dropped sharply due to which hypoglycemia
developed — a decrease in the blood glucose level below the
normal value (below 3.3 mmol / l), she explains pallor of
kozh.pokrov, as well as a cold man (because sweating increases).
- observed in diabetes
2) Why is there a loss of consciousness in this condition and what
is the reason for the presence of the meter and syringe in the
patient’s pocket?
- reaction of the central nervous system to decrease ur-glucose in
the blood and inhibit the exchange of matter in the brain; first
reacts - the cortex, then the cerebellum (coordination); medulla -
coma.
- insulin overdose → hyperinsulinemia → hypoglycemia → energy
starvation (substrate hypoxia) → disturbed pattern. ATP →
damage to neurons → coma
- so that the glucometer is a device for measuring the level of
glucose in organic liquids (blood, cerebrospinal fluid, etc.), is used
to diagnose the state of carbohydrate metabolism in people
suffering from diabetes. The syringe is used for insulin injections in
diabetic patients.
3) What first aid is needed and why?
- first aid - to give the patient a solution of sugar, any sweet drink
inside, food rich in carbohydrates (sugar, honey can be under the
tongue).
- if possible, enter glucagon intramuscularly, 40% solution of
glucose in / in with the preliminary introduction of subcutaneous vit
vit B1 - prevention of local muscle spasm.
Task №35
A patient with severe jaundice and complaints of weakness, fever
(+ 38.5C) was admitted to the infectious diseases department of
the hospital. Concentration of direct and indirect bilirubin
increased. In the urine, direct bilirubin and urobilin. What type of
jaundice is it?
1) Provide a scheme for the formation of direct and indirect
bilirubin.
2) Write the conjugation reaction of indirect bilirubin and list the
properties of direct and indirect bilirubin.
3) Indicate the activity of which liver enzymes are determined in
the blood for the diagnosis of liver pathology and describe the
basic principles underlying enzymodiagnosis.
The patient has parenchymal jaundice
1)
2)
Indirect Bilirubin
 Toxic
 Gives a reaction with Ehrlich diazoreactive in the presence of
alcohol
 Normally, the serum content does not exceed 3-16 µmol / l
 Does not appear in the urine
 Fat soluble
 Not linked to glucuronic acid
"Direct" bilirubin
 Non toxic
 Gives a direct reaction with Ehrlich diazoreactive
 It is only in the bile
 Appears in urine
 Soluble in water
 Coupled with glucuronic acid
3) With the defeat of the liver, the enzymes from the cells are
washed into the blood, and their activity increases. The greatest
diagnostic value is the determination of the activity of ALT and
AST. The activity of transaminases in serum: AsAT - 5 - 40 U / l,
AlAT - 5 - 43 U / l. In acute parenchymal hepatitis, AlAT increases
by 20–30, and sometimes 100 times or more. AcAAT activity
increases slightly less.
Enzymodiagnostics is a study of the activity of enzymes of blood
plasma, urine, and saliva in order to diagnose certain diseases.
Changes in specific enzymatic processes can be the cause or
effect of various pathological conditions. Most enzymatic
processes are localized inside the cells, but determining the
activity of enzymes outside the cellular environment (serum,
plasma, saliva, urine) may have diagnostic value.
Task №36
The patient complains of breaking pain in the lower third of the leg.
Recently, losing weight and a sharp weakness. The doctor assumes
that the patient has a bone damage. What is this assumption based
on?
1. What specific enzymes need to be determined in a patient to
confirm the localization of bone damage?
2. What macroelements should be determined in the blood in
this case?
3. What hormones can be determined in a patient to clarify the
diagnosis and prescription of therapy, indicate their physiological
effect?
1) Acid phosphatase - concentrated in osteoclasts, participating in bone
resorption, catalyzed the reaction of the splitting of organic phosphate
esters with the release of phosphate ions.
Lysosomal - participate in resorption of bone tissue (9 hydrolases:
aminopeptidase, beta-glucuronidase, galactosidase, collagenase,
phosphoamidase, nucleotidase, KF)
In general, bone mineralization is characterized by the interaction of
three factors:
1. Local increase in the concentration of phosphate ions;
2. Ca2+ adsorption of ions;
3. Shift of PH
1. Alkaline phosphatase plays a large role in the process of ossification.
It is found in both osteoblasts and osteoclasts. Alkaline phosphatase is
involved in the formation of the main organic matter of bone and
mineralization. One of the mechanisms of its action is a local increase
in the concentration of phosphorus ions to the point of saturation,
followed by the fixation of calcium-phosphorus salts on the organic
matrix of bone.
 During the reduction of bone tissue after fractures, the
content of alkaline phosphatase in the callus increases sharply.
 In violation of bone formation, a decrease in the content and
activity of alkaline phosphatase in bones, plasma and other tissues
is observed.
 During rickets, which is characterized by an increase in the
number of osteoblasts with insufficient calcification of the main
substance, the content and activity of alkaline phosphatase in the
blood plasma increase
2)
 Inclusion of Ca2+ in bones is an active process. This is
clearly proved by the fact that living bones perceive Ca2 + more
intensely than strontium. After the death of such selectivity is no
longer observed. The selective ability of bone in relation to calcium
depends on temperature and is manifested only at 37 ° C.
 PH value plays an important role in the mineralization
process. With an increase in pH, calcium phosphate is deposited
more quickly in bone tissue. There is relatively much citrate in the
bone (about 1%), which affects the maintenance of pH.
3)
 Calcitonin is a hormone of peptide origin, produced
predominantly by parafollicular C-cells of the thyroid gland, as well
as other organs in small quantities, especially the development in
the lungs.
Calcitonin receptors are detected on osteoclasts, monocytes, in the
kidneys, brain, pituitary, placenta, gonads, lungs and liver. Calcitonin
exhibits a hypocalcemic effect due to a decrease in osteoclast activity
and a decrease in the rate of osteolysis of bone tissue, a decrease in
the absorption of calcium in the kidneys, and a decrease in calcium
absorption in the intestine. It reduces renal osteolysis of phosphates,
causing a moderate decrease in blood phosphorus. According to its
functional characteristics, calcitonin is an antagonist of parathyroid
hormone, however, its role in the regulation of calcium-phosphorus
metabolism compared to parathyroid hormone in the human body is
small.
 Parathyroid hormone (parathyroid hormone, parathyrin, PTH)
is a parathyroid hormone that regulates the level of calcium and
phosphorus in the blood. Function of parathyroid hormone is the
deposition of calcium in the bones with its excess in the blood.
Violation of the release of parathyroid hormone, has a negative effect
on the phosphorus-calcium metabolism of the body, due to the loss of
calcium by the kidneys, violations of its absorption by the intestines and
leaching from the bones.
Excess parathyroid hormone is characterized by slowing the formation
of bone tissue, while the old bone beams actively dissolve, leading to
bone maceration - osteoporosis. The density of bones and their
strength is reduced, which threatens with frequent fractures, but the
level of calcium in the blood will be elevated, as calcium under the
action of the hormone is washed into the plasma.
Task №37
In the emergency room of the hospital entered the patient with
acute inflammatory phenomena in the joints and the heart. What
spectrum of biochemical analyzes should be assigned to a patient
in this case?
1) What changes in serum protein fractions can we expect in acute
inflammation?
2) How do protein fractions change when chronization of
inflammation?
3) Name the proteins of the acute phase and give them a brief
description.
1. In serum protein fractions increase in α1- and α2-globulin
fraction that is associated with acute and subacute
inflammatory processes and some malignant tumors,
injuries, because This includes most of the proteins of the
acute phase (C-reactive protein, α2-macroglobulin, α1-
glycoprotein, α1-antitrypsin, ceruloplasmin, haptoglobin).
Alpha-1-globulins in the blood from 2 to 5% (2.1-3.5 g / l)
C-reactive protein (CRP) is the most sensitive and quickest
indicator of tissue damage during inflammation, necrosis,
trauma; reacts precipitation with pneumococcal C-
polysaccharide. Stimulates immune responses,
phagocytosis, activation of the classical systemic
complement.In a healthy person, it is absent, it is
synthesized in hepatocytes.
SAA protein - amyloid protein A - is the N-terminal part of its
serum precursor mol. mass 90000. This precursor belongs to
the proteins of the acute phase, its concentration in serum
increases sharply in response to tissue damage or
inflammation. The level of the precursor of amyloid protein A
increases with age and, when it reaches high values,
amyloidosis can develop.Synthesized in the liver; fast and
strong marker of "acute phase", amyloidosis, stroke
Fibrinogen is a valuable indicator of hemostasis
(coagulogram). Fibrinogen - a protein produced in the liver
and turning into insoluble fibrin - the basis of a clot during
blood coagulation. The content of fibrinogen in the blood
increases with the onset of acute inflammatory diseases and
tissue death. Fibrinogen affects the erythrocyte
sedimentation rate
2)In protein fraction increase content of gamma globulins
The gamma fraction contains immunoglobulins G, A, M, D,
E. Therefore, an increase in the content of gamma globulins
is observed in the reaction of the immune system when
antibodies and autoantibodies are produced: in viral and
bacterial infections, inflammation, collagenosis, tissue
destruction and burns. Significant hypergammaglobulinemia,
reflecting the activity of the inflammatory process, is
characteristic of chronic active hepatitis and liver cirrhosis.
3)The acute phase proteins are a large group of serum
proteins (mainly α-globulins) with various functions combined
according to a common feature — a rapid and significant
increase in the concentration during bacterial, viral, parasitic
infection, physical or chemical injury, toxic or autoimmune
reaction, malignant neoplasms. The meaning of this increase
is to increase the body's resistance to free-radical reactions,
to limit tissue damage, to suppress the rate of reproduction
of bacteria.
Alpha1 globulins include:
- α1-antitrypsin
- α1-glycoprotein
Alpha2 globulins include:
- ceruloplasmin
- haptoglobin
- α2-macroglobulin
The acute phase proteins include:
 C-reactive protein,
 serum amyloid A,
 haptoglobin-glycoprotein, which is 25% of alpha-2-
globulin fraction, a transport protein. The main function
is plasma binding of free hemoglobin, a hemoglobin-
haptoglobin complex with a high molecular weight is
formed, this complex does not pass through the renal
filter (like free HB) and iron is not allowed to pass
through the kidneys. Haptoglobin increases with all
reactions of the acute phase - the active form of
tuberculosis, pneumonia, collagenosis, GI disease,
lymphogranulomatosis, osteomyelitis, AMI, sepsis,
purulent processes
 α2-macroglobulin-α2 - Macroglobulin is a high
molecular weight zinc protein, contains 4 identical
subunits and includes a carbohydrate component.
Protein is synthesized in the liver and in
immunocompetent cells. An increase in its level is
detected in cirrhosis of the liver, acute and chronic
hepatitis, endocrine diseases (diabetes mellitus,
myxedema), during pregnancy and treatment with
estrogens, and nephrotic syndrome.
 ceruloplasmin-the main copper-containing blood
protein, which plays an important role in the
metabolism of iron and is related to alpha-2-
globulins.An increased amount of ceruloplasmin is
formed during the acute stage of infectious
pathologies. It is necessary to combat pathogens.
Hence the name - acute phase protein.
 α1-glycoprotein-is one of the main proteins of the
"acute phase". Serum concentration can increase by 3-
4 times in inflammatory processes, infections,
malignant tumors.
 α1-antitrypsin-liver protein, the main role of which is to
inactivate protease enzymes that break down
connective tissue in the body.Increased due to acute
inflammatory diseases, chronic inflammatory diseases,
acute hepatitis, chronic hepatitis, alcoholic cirrhosis
and others
 orosomucoid-it is a substance that belongs to the
“slow” proteins of the acute phase of inflammation. Its
content in the blood is rarely determined, since there
are more reliable markers of inflammation. Increased
rates are characteristic of acute phase of inflammation
(infection, tissue damage), extensive malignant
neoplasms, the risk of cardiovascular disease in
patients with type 2 diabetes,connective tissue
diseases.
 Complement components C1-C4, C9-proteins of the
complement system, belong to BOP, during
inflammation their activation - lysis of foreign cells,
however, their content can often decrease, because
together with other proteins the complement is spent
on opsonization and lysis of cells (RA, rheumatism,
cardiovascular disease), Enteropathies,
transplantations are secondary insufficiency of SC
proteins, thus the inflammatory reaction causes a
significant increase in the whole class of glycoprotein
proteins, being inhibitors and deactivators of those
substances that are released during damage.
Transferrin is also referred to as the acute phase proteins, but its
concentration during inflammation decreases - it is called the
negative protein of the acute phase.
Task №38
The patient complains of recurrent and shingles abdominal pain,
especially severe in the left hypochondrium. Recently appeared
frequent and loose stools, especially after taking fatty foods. In
feces the presence of fat. The doctor assumes the defeat of the
pancreas. What is this assumption based on?
1. What specific enzyme rises in the blood in acute lesions of
the pancreas. What class and subclass is it?
2. Why, after taking fatty foods in this case, is there a frequent
liquid stool and there is a lot of fat in it?
3. What substances are needed to activate the pancreatic
enzyme that hydrolyzes food triglycerides, where they are
produced, their role?
The main symptoms of acute pancreatitis (inflammation of
pancreatic tissue) are: loose stools; severe pain in left
hypochondrium, nausea and vomiting.
1. lipase is an enzyme that is synthesized in the pancreas, is
released into the lumen of the 12th finger and small intestine,
where it breaks down food fats (TAG → into glycerol and
fatty acids). When pancreatitis rises and remains at this level
for 12 days.
- hydrolase - esterase - lipase
2) lack of LIPOFIL enzymes affects the digestion of fat -
feces become fatty and plentiful.
3) pancreatic lipase is displayed in the 12th peristhirk in the
form of inactive proenzyme - prolipase. The activation of
prolipase in active lipase occurs under the action of bile
acids (phosphatidylcholine, cholesterol) and the enzyme
pancreatic iron-lipocolipase.
Bile acids are formed in the liver from cholesterol. Role:
1. Strengthens intestinal perepalhtiku
2. Provides fat digestion: - emulsification, - formation of
micelles.
3. Excretion of excess cholesterol, bile pigments,
creatinine, metals, drugs.
Task №39
A 40 years old man came to the doctor with complaints of severe
sweating, the wife of the patient noticed that his features were
blunt, recently he had to buy shoes of bigger size. The doctor
found moderate hypertension and glucosuria. A patient was sent to
the endocrinology department for examination. What hormonal
violation can be assumed in the patient and what are the listed
signs related to?
1) What hormones should be detected in the blood of a given
patient? Why? What kind of changes are expected?
2) Explain the molecular mechanisms of glycosuria in this case.
3) Describe the physiological effects of the hormone to which the
data is associated.
1)It is necessary to determine the hormone GH (STH) in the blood.
Because with an increase in the blood of this hormone may be
excessive sweating.
2)STH with a long-term exposure in large doses shows a
diabetogenic effect, that is, growth hormone increases glucose
production by the liver and reduces the uptake of glucose by the
tissues. As a result, an excess amount of glucose appears in the
blood, as a result, glucose reabsorption is disturbed and glycosuria
is observed.
3)Mechanism of action. St increases synthesis of somatomedins in
liver and other organs, they posses insulin similar action, their
mechanism action II: -I (cAMP), +I (cGMP), permeability of
membranes for glucose, amino acids, purine and pyrimidine
bases.
Target cells – all tissues.
Physiological action:
1. Oxidation of glucose increases;
2. Lipolysis oxidation increase synthesis of ketones increase;
3. division of cartilage cells , increase;
4. synthesis of proteins increase;
5. rate of growth of bones Increase,
cartilage and their mineralization growth (somatomedin A,C);
6. Ca++ and P in the blood inc;
7. cAMP in pancreasglucagon inc inc;
8.synthesis of somatomedins inc. There are 7 somatomedins: A
(2), B (4), C. A and C:
1) division of cartilage cells inc;
2) synthesis of DNA, RNA inc;
3) synthesis of protein, especially of proteoglycans inc; C – acts
as insulin .; B - synthesis of DNA and protein in brain inc.
In the finish of pregnancy the synthesis of somatotropin
increases®temporary acromegalia. Hyperproduction of St in
childhood evokes the development of gigantism, in adult –
acromegalia. Hypoproduction of St in childhood evokes the
development of dwarfs. The treatment of dwarfs – 10 mg St/kg – 3
times in day causes the increasing of growth on 10-20sm/year.
Task №40
The girl went to the doctor with complaints of excessive sweating,
protrusion of the eyes and weight loss, although the appetite didn’t
suffer. On examination, an enlarged thyroid gland was observed.
What hormonal disorder can be assumed in this patient? What are
the reasons of listed signs? Explain the answer.
1. What hormones should be detected in the blood of this
patient? Why? What changes should be expected?
2. Indicate the physiological effects of the hormones involved in
the pathological process in this case.
3. Show schematically the process that is disturbed in this
patient and which one is the reason of sweating?
The diagnosis of this patient is hyperthyroidism (Graves’ disease)
The excessive sweating is explained by the fact, that an increase
in the amount of thyroxine causes an increase in permeability and
a decrease in the electrical resistance of the mitochondrial
membranes and, therefore, a disconnection of biological oxidation
and oxidative phosphorylation occurs. As a result, ATP synthesis
is reduced. Oxidation energy not used for oxidative
phosphorylation is released in the form of heat, because of this, in
such patients, the body temperature increases by 0.5-1°C and the
process of sweating intensifies.
Protrusion of the eyes (Exophthalmia) occurs due to edema of
retrobulbar cellulose (endogenous water) and dysfunction of the
oculomotor muscles due to changes in the tone of the vegetative
nervous system.
Weight loss occurs due to a sharp increase in the breakdown of
lipids and proteins. The same can explain the preservation of the
patient's appetite.
The appearance of a sign of an enlarged thyroid gland is explained
by hypertrophy and hyperplasia, the need for large quantities of
iodine for the increasing synthesis of hormones during
hyperfunction of the gland. Iodine comes with blood in normal
doses, therefore, the mass of the gland rises compensatory in
order to take as much as possible iodine coming with blood.
1. a) Thyroid-stimulating hormone (TSH)
Mechanism of action: 1st trough cAMP
Target-cells: thyroid gland and fat tissues
In the blood test, a low level of TSH is expected, which indicates
the increased thyroid function that produces too many thyroid
hormones.
b) Total and free T (Thyroxine)
4
Mechanism of action: Almost all of the T hormones turn into T ,

4 3
because of this, talking about the effect of this hormone in normal

is not right.
Target cells: most cells have receptors for thyroid hormones,
except spleen and testes. Especially many receptors are in heart,
liver and hypophysis cells.
Free thyroid hormones T penetrate into the cells of the body,
4
where they turn into T , the active part of thyroid hormone.

3
Total thyroid hormone T measurement is used as an additional
4
indicator.
In the blood test the high level (above normal) of T is expected.
4
c) Total and free T (triiodothyronine)

3
Mechanism of action: 2nd through cGMP

Target cells: same as for T 4
In the blood test, the level of T is also expected to be higher than

3
normal.
2. Thyroid-stimulating hormone:
1) Participates in all stages of thyroid hormones synthesis:
· Promotes tyrosine iodization;
· Promotes the synthesis of thyroglobulin;
· Promotes the production of T and T ;
3 4
· Releases hormones from thyroglobulin;

· Promotes the release of hormones in blood.
2) Enhances lipolysis and glycogenolysis in target cells;
3) Stimulates the vascularization of thyroid gland, increases the
amount and size of the follicle cells of the thyroid gland.
T and T - Affect the metabolism of protein, lipids and
3 4
carbohydrates in target cells.
3.
Task №41
The patient has frequent infectious diseases, poor wound healing.
In the study of protein fractions in the serum detected: albumin -
60%; alpha-1 globulins - 5%; alpha-2-globulins - 10%; beta
globulins - 12%; gamma globulins - 13%. What does the result of
electrophoretic blood serum in this case indicate?
1. What are the normal indicators of serum protein fractions?
2. Show the normal chemical composition of blood plasma and
indicate the role of gamma globulins in the body.
3. What is the essence of the electrophoresis method? List the
chemical properties of globulins
1. Normal indicators of protein fractions in serum: albumin -

55.8 - 66.1%, alpha-1-globulin - 2.9 - 4.9%, alpha-2-globulin -
7.1 - 11.8%, beta-globulin - 4.7 - 7 , 2%, gamma globulin -
11.1 - 18.8%
2. Blood plasma consists of water (90–93%) and dry residue (7-
10%). The composition of the dry matter includes proteins,
carbohydrates, lipids, electrolytes, organic acids and bases.
From 7-10% of the dry residue, 6.6-8.5% are plasma
proteins, and the remaining 1.5-3.5% are organic substances
(carbohydrates, lipids, nitrogen-containing products of
protein catabolism) and mineral compounds (Cl-, Na +, K +,
Ca2 +, HCO3, etc.).
Gamma globulins contain protective antibodies that can
neutralize the pathogenic effect of various microorganisms.
Gamma globulins have a detrimental effect on viruses,
bacteria, spirochetes and protozoa, which determines their
important role in the prevention and treatment of a number of
inf. diseases
3. Proteins and other charged macromolecules can be
separated by electrophoresis. Among the various
electrophoretic methods, the most simple is electrophoresis
on a carrier, especially on the cellulose cellulose film. In this
case, whey proteins, which due to the presence of an excess
negative charge move to the anode, are divided into the five
aforementioned fractions.
Globulins make up 40% of all plasma proteins. Globulins - a
heterogeneous fraction of proteins. The content of α1-
globulins is 4%, α2 - globulins - 8%, β-globulins - 12%, γ-
globulins - 16%. The molecular mass of globulins is about
200 thousand d. They are less hydrophilic, dissolve in 10%
salt solutions, 50% (NH4) 2SO4 are precipitated. Globulins
are synthesized in the liver, lymphocytes, macrophages. The
main functions of globulins include transport, protective
functions.
In the composition of the globulin fraction, individual proteins
are isolated: Proteins of α1 - globulin fraction, Proteins of α2-
fraction of globulins, Proteins of β - fraction of globulins
Task №42
Irina K., 35 years old, on the advice of an acquaintance physician,
excluded all carbohydrates from her diet. She was prompted by the
problem of an increase in blood glucose, which began as a result of a
strong experience that lasted one week. After a week of such a diet,
she noticed a decrease in body weight (weight loss), but the glucose
level did not return to normal. She continued to exclude all
carbohydrates from the diet, and after a month of such a diet her weight
was 30% lower than the initial one, the smell of fruit essence appeared
from the mouth.
Additional complaints:
- frequent urination;
- burning of the tip of the tongue, hoarseness of the voice, appearing
after eating;
-black dots before eyes.

1) What indicators should be assigned to the study to exclude or
confirm the presence of diabetes?
2) What hormones are involved in the stress response and increase
blood glucose levels? Indicate the normal level of glucose in the blood,
list these hormones and list their place of formation. Show the
mechanism of their hyperglycemic action.
3) What is the reason for the smell of fruit essence from the mouth of
this patient? Show schematically the reactions of formation of
substances that are supposed to cause this smell. Where are they
formed and what is their role in a healthy body?
1) For the diagnosis of diabetes, you need to check the amount of:
glycemia, glycated hemoglobin, fructosamine, C-peptide.
2) Cortisol is an important hormone that is released by the adrenal
glands in response to stress and affects many functions in the body,
including an increase in blood glucose levels.
Cortisol increases glucose levels by synthesizing glucose from proteins
(gluconeogenesis) and reducing the uptake of glucose by the cells of
the body. Cortisol also contributes to the breakdown of fats to free fatty
acids, from which ketones can be created.
Normal blood glucose is 3.4-6.1 mmol / l.
Adrenaline is a stress hormone secreted by the adrenal glands.
Adrenaline increases blood glucose levels, primarily due to the
destruction of glycogen in the liver. Adrenaline concentration rises
when the body is exposed to stress, fever, or acidosis. Adrenaline also
lowers the uptake of glucose by the cells of the body.
3) The body of a patient with diabetes mellitus cannot use glucose as
an energy source; therefore, it switches to lipid breakdown products -
ketone bodies. Ketone bodies form a lot, then in the bloodstream, they
cause hyperketonemia, ketoacidosis, ketonuria. In patients with
diabetes mellitus, acetone is formed from acetoacetic acid more than in
a healthy person, so there is a smell of fruit essence from the mouth, it
even smells like skin. The formation of acetone can be considered a
compensatory phenomenon, as the body is protected from an excess
of acid-reactive acetoacetic acid.
Ketone bodies are synthesized in the liver mitochondria from AAA,

which is formed during β-oxidation of fatty acids. Ketone bodies include
acetoacetic acid, β-hydroxybutyric acid and acetone.
*With prolonged fasting, diabetes mellitus increases the content of
acetoacetate in the blood, which decarboxylates non enzymatically and
turns into acetone.
Task №43
The patient is overweight, complains of shortness of breath,
aggravated by physical exertion, the appearance of xanthomas on
the eyelids and other parts of the body. Eats mainly fast food (food
rich in easily digestible carbohydrates, starch, animal fats). What
laboratory parameters should be determined in this patient?
Explain the signs listed in this case from the biochemical point of
view. Reason the answer.
1. Name the transport forms of lipids and show their
metabolism schematically.
2. Specify normal values of total cholesterol, triglycerides and
glucose for an adult healthy person.
3. What recommendations regarding diet you give to this
person?
Task №44
The patient has a sharply increased blood pressure, basal metabolic
rate, sugar content, and the level of free fatty acids in the blood. The
amount of adrenaline and norepinephrine in the blood plasma
increased 500 times. Which organ pathology can you think of?
Algorithm of decision:
1. Name the place of production of adrenaline and
norepinephrine.Show schematically the formation of this hormones.
2. What mechanism do these hormones act on? What enzymes
are active under the influence of these hormones?
3. Explain the mechanism of the disease manifestations below.
An increase in the content of norepinephrine and adrenaline may be
associated with a tumor of the adrenal medulla. Catecholamines have a
powerful vasoconstrictor,hyperglycemic, lipid-mobilizing effect, which
explains the above-mentioned changes in the body.
1. Adrenaline is produced exclusively in the adrenal medulla,
because only they have a specific methyltransferase that
accelerates the methylation of norepinephrine to adrenaline. In turn,
the synthesis of methyltransferase in the medulla is controlled by
glucocorticosteroids and, before getting into the general circulation,
glucocorticoids in high concentration pass through the medulla.
Under the action of a nerve impulse, adrenaline is released from
these granules by exocytosis, which enters the extracellular
environment, then into the blood. Norepinephrine can be
synthesized in many organs, at the end of the sympathetic nervous
system.
Catecholamines are synthesized from the amino acids
phenylalanine of tyrosine.
2.
The mechanism of action -is the first. Receptors to which
catecholamines can join are of two types: a- (a1 and a2) and b- (b1, b2
and b3) -adrenoreceptors, their density on the surface of cells of
various organs and tissues is different. In particular, b-receptors in
large quantities are found on the cells of the blood vessels of the brain,
heart, liver, adipose tissue. There are many a-receptors in the intestinal
vessels, peripheral vessels, in the abdominal organs, with the
exception of the liver. Catecholamines, by binding to a1 receptors,
accelerate the accumulation of cGMP, activate phospholipase C, which
leads to an increase in IP3 and DAG.Catecholamines, binding to a2-
adrenoreceptors, help reduce the formation of cAMP, and interacting
with b-receptors, stimulate the formation of cAMP. Therefore, the same
hormone, acting through different receptors, can cause the opposite
effect: the formation of the hormone-a-receptor complex accelerates
the synthesis of glycogen and lipids, and the hormone-b-receptor
complex causes their breakdown. The physiological effect of hormones
on the walls of blood vessels, especially coronary and cerebral, is also
different: vasoconstriction causes the hormone associated with the a-
receptor, and expansion - associated with the b-receptor.
It is also known that norepinephrine has a high affinity for a1 and β1
receptors, and adrenaline - for α2 and b2 receptors. In this regard, their
effect on organs and tissues is different. It is also known that at high
concentrations adrenaline can interact with a-receptors.
Target cells- are the liver, skeletal and cardiac muscles, adipose tissue,
the central nervous system, the muscles of the vessels, bronchi,
intestines, urinary tract.
Physiological action: since adrenaline promotes the formation of cAMP
AMP, glycogenolysis increases in target cells. Glucose-6-phosphate
molecules formed in the liver are dephosphorylated and glucose enters
the blood. In the muscles, glucose-6-phosphate (due to the absence of
the enzyme glucose-6-phosphatase) undergoes glycolysis and is used
as an energy source; more often, glucose in the muscles breaks down
to lactic acid, which enters the liver and is used for
gluconeogenesis.Under the action of adrenaline, the absorption of
glucose by muscles and other organs and tissues is reduced due to a
decrease in insulin secretion, which prevents the consumption of
glucose by the tissues, saving it for the brain.
In adipose tissue, liver lipolysis increases, the released FFA in liver

cells undergo b-oxidation, ketone bodies form in increased amounts,
which enter the blood and then into muscles and burn in these cells.
Glycerin is also used for gluconeogenesis.
Expansion of cardiac vessels, brain tissue improves blood supply to

these organs, contributes to better tissue energy supply, increases
oxygen consumption, increases redox processes, as a result of which
the efficiency of cardiac and skeletal muscles increases. So, adrenaline
brings the body into a state of readiness to fight, speeding up the heart
rhythm, increasing cardiac output and increasing blood pressure, thus
preparing the cardiovascular system for activity in an extreme situation.
Adrenaline has a cardiotonic, hyperglycemic, caloric effect, because
contributes to the maximum provision of organs and tissues, in
particular the nervous system and muscles, easily utilized by energy
substrates - glucose and ketone bodies. This leads to an increase in
the use of oxygen by the tissues and an increase in the metabolism, an
intensification of tissue respiration.
Norepinephrine, acting through a-receptors, narrows the vessels of the
abdominal cavity and peripheral arteries. This increases blood
pressure. Adrenaline, acting through b-receptors, dilates the vessels of
the brain, liver and heart. As a result, the blood flow in these organs
improves. Thus, under the action of catecholamines, under stress,
there is a redistribution of blood flow, which increases the adaptive
ability of the body to the effects of stress.
3. The cause of high blood pressure is stress and constant experience.

Also, hypertension can develop in people who are genetically located
for this disease. The environment plays a significant role in the
development of hypertension.
Causes of high blood sugar
Blood glucose levels may vary:
Short-term physiological processes in the body (increased physical
exertion, stressful situations), which is associated with an increase in
energy metabolism in the cells or when eating large amounts of
carbohydrates in food;
Persistent high blood sugar may occur:
with pathological processes of the gastrointestinal tract.
in inflammatory diseases of the endocrine glands (pancreas,
hypothalamus, adrenal glands and pituitary.
Also one of the causes of persistent and prolonged increase in blood
sugar is diabetes.
In patients with insulin deficiency, lipase activity increases, which leads
to an increase in lipolysis and an increase in the concentration of fatty
acids in the plasma and liver. The content of glucagon in such patients
also increases, and this also enhances the release of free fatty acids in
the blood.
Task №45
During the examination of the workers of the “Dry Cleaning”
association, one of the workers had an increase in ALT activity in
the blood of 5.7, and AST by 1.5 times. What is the presumptive
diagnosis you can make this patient? How does the color of urine
and feces change in a patient?
1. What types of jaundice are there? The reasons for their
occurrence.
2. A picture of blood, urine and feces in this pathology.
3. What additional tests should be assigned and what possible
deviations can be expected in them?
According to the examination results, the presumptive diagnosis in
this patient: Acute toxic hepatitis. As a result of this disease, the
level of ALT and AST in the blood increases, while the level of ALT
increases more than AST. This is due to the fact that the enzyme
ALT has a specific organ localization in the liver and when cells
break down, it enters the bloodstream, where its activity increases
sharply, which is observed in the patient.
1. There are several types of jaundice:
1. Mechanical (Obstructive), subhepatic jaundice
Associated with the termination of the flow of bile into the intestine.
Causes: any processes that impede the outflow of bile:
- cholelithiasis
- pancreatic head tumor
- inflammatory process in the bile ducts
Result: Increase in blood of total bilirubin due to direct.
2. Hemolytic (subhepatic) jaundice
Occurs with increased erythrocyte hemolysis.
Causes: - incompatible blood transfusion
- infectious diseases
- chemical intoxication
Result: Increase in blood total bilirubin due to indirect, which does
not have time to be neutralized in the liver.
3. Parenchymal (hepatic) jaundice
Occurs when liver cells are damaged and is accompanied by
increased permeability of hepatocyte membranes.
Causes: - viral diseases
- toxic drugs
Result: Increase in blood total bilirubin due to both direct and
indirect.
4. Physiological jaundice
It occurs in newborns, the intensity of which normally begins to
decrease on the second day, and after two weeks passes.
Causes: - increased disintegration of fetal hemoglobin (HbF), when
changing to adult hemoglobin (HbA).
- insufficiency of formation of glucuronyltransferase,
bilirubin neutralizing enzyme.
2. In this pathology, urobilinogen is increased in the urine
because hepatic damage decreases the enterohepatic
circulation of this compound, allowing more to enter the
blood, from which it is filtered into the urine. The urine
consequently darkens, whereas stools may be a pale, clay
color, depending on the damage level of the liver.
Blood serum becomes darker due to an increase in the level of
direct and indirect bilirubin in the blood.
3. - Study on the activity of ALT, AST (increases)
- Study on the amount of bilirubin (increases)
- Abnormal protein-sediment samples
- Impaired liver production of fibrinogen, prothrombin, VII, V
coagulation factors.
Task №46
In patients with severe viral hepatitis, hepatic coma may develop,
due, in particular, to the toxic effect of ammonia on brain cells.
What is the reason for such a significant accumulation of ammonia
in the blood? How will the urea concentration change in the blood
of these patients? What biochemical parameters should be
determined in patients with hepatitis to prevent and early detection
of this complication?
1. Name the ways of formation and neutralization of ammonia.
2. What are the main mechanisms of the toxic effect of
ammonia on brain cells?
3. What liver tests are carried out to study abnormal liver
function?
In the large intestine a significant amount of ammonia is formed,
which is a product of decay with the action of intestinal bacteria on
nitrogenous substrates. Ammonia is absorbed into the portal
blood, but under normal conditions in the liver, some of the
ammonia formed is converted into urea and is quickly removed
from the body. In liver diseases, the function of hepatocytes
(antitoxic function of the liver) may be impaired, the synthesis of
urea is inhibited, and in this case, the concentration of ammonia in
the peripheral blood rises to toxic levels.
Required tests to identify hepatic coma:
 viral hepatitis markers
 blood bilirubin concentration (hyperbilirubinemia)
 determination of the amount of serum transaminases
(increases)
 determination of prothrombin index and thrombocyte count in
the blood (decreases)
 determination of the amount of ammonia in arterial blood and
cerebrospinal fluid (increases)
1. Ways of ammonia formation:
 the disintegration of pyrimidine bases
 deamination of amino acids
 hydrolytic deamination of purine bases
 deamidation of amides
 deamidating of hexosamines
 neutralization of biogenic amines
Ways of ammonia neutralization:
 Amidation (in all tissues except liver)
In the human body, the process of amidation occurs with
glutamic and, less commonly with aspartic acids, which,
when released into the liver, undergo deamidation.
Consequently, the formation of amides is a temporary
neutralization of ammonia and its transport form:
 Ammoniogenesis (in kidneys)

In the kidneys, a part of the formed ammonia goes to
neutralize acidic products and is eliminated from the body in
the form of ammonium salts:
 Reductive amination (in the liver)
A part of ammonia interacts with α-ketoglutaric acid to form
glutamic acid, that is, it participates in the reductive
amination reaction:
α-ketoglutaric α-iminoglutaric
α-aminoglutaric
 Urea biosynthesis (in the liver)
The formation of urea in the liver cells is carried out
according to the Krebs theory (ornithine cycle).
3АТP 3АDP
NН + СО + ЗН О + Asp
3 2 2 urea + fumarate+
3Н РО
3 4
general urea formation scheme

2. In small concentrations, ammonia is a physiological irritant,
and in large quantities it is toxic, including for the central
nervous system. This is explained by the fact that ammonia
passes through the membranes of brain cells with blood and,
once in the mitochondria, ammonia interacts with α-
ketoglutarate to form glutamate; This reaction is the inversion
of the glutamate dehydrogenase reaction:
The result is ultimately the outflow of α-ketoglutarate from the pool

of intermediate products of the citric acid cycle in brain
mitochondria and, as a result, a decrease in the rate of glucose
oxidation, which plays the role of the main fuel for brain cells.
3. Liver function tests for liver function disorders:
 Blood bilirubin concentration (total, direct, indirect)
 The number of ALT and AST
 GGT (gamma-glutamyl transpeptidase)
 alkaline phosphatase
Task №47
A patient with kidney disease, despite a balanced diet, renal
osteodystrophy has developed - a rickets-like disease,
accompanied by intensive bone demineralization. Why damage
kidney disease in this patient led to demineralization? What are the
blood and urine indicators should be determined in a patient to
clarify the diagnosis and correction of therapy? What kind
hormones can be recommended to determine the patient?
1) What is the connection between the development of rickets and
kidney disease?
2) What biochemical indices are determined in blood and urine
with
rickets and kidney disease?
3) What hormone levels will increase or decrease with bone
demineralization?
1. The main factors for the development of Renal
osteodystrophy(ROD) are a violation of Ca-P homeostasis, the
metabolism of vitamin D and Parathyroid hormone, as well as
changes in the somatotropic axis. In recent years, the ROD
spectrum has been recognized to include conditions with “high”
and “low” bone metabolism. As a result of the Chronic renal failure
itself, and as a result of the treatment of ROD, a high plasma level
of phosphorus is formed and the product of Ca´P increases. Both
of these indicators are important risk factors for the development of
vascular calcification, cardiovascular morbidity and mortality in
young people who have been in childhood Renal replacement
therapy (RRT) since childhood.
In the kidneys, the process of hydroxylation proceeds in the first
position of 1,25-deoxycholecalciferol, one of the active metabolites
of vitamin D (calciferol). This metabolite is involved in the
homeostatic regulation of calcium metabolism and osteogenesis.
Namely: regulates the processes of absorption of Ca and P in the
renal tubules, bone resorption and reabsorption of Ca and P in the
renal tubules.
The progression of nephrosclerosis with chronic kidney disease
deepens the violation of the hydroxylation of calcidiol, resulting in
reduced or completely suppressed production of the effective form
of vitamin D3 - dihydroxycholecalciferol. This leads to a decrease
in calcium absorption in the small intestine and reabsorption in the
kidney according to hypocalcemia, which is a powerful stimulator
of PTH secretion, and consequently, the development of
hyperparathyroidism.
2. Biochemical examination of urine:
-study of excretion of amino acids in the urine - increased
excretion (hyperaminoaciduria) - one of the early laboratory signs
of rickets
-study of urinary calcium excretion - it is known that vitamin D
deficiency leads to suppression of urinary calcium excretion
-urine sample according to Sulkovich
-Quantitative determination of calcium in a single (first or second
morning portion) or daily urine
-determination and calculation of calcium-creatinine ratio - the ratio
of calcium to creatinine in the analyzed (usually in the first or
second morning, perhaps in the daily) urine
Biochemical study of blood.
-total protein content - dysproteinemia, hypoproteinemia;
-total alkaline phosphatase activity (its bone isoenzyme)
-calcium content - normal content or decrease in total calcium
concentration (up to 2 mmol / l and below), ionized calcium (up to
1 mmol / l and less) is observed
3. The balance of calcium and phosphorus in the body is a
complex process that is regulated by such biologically active
compounds as vitamin D, parathyroid hormone (PTH) of the
parathyroid glands and calcitonin C-cells of the thyroid gland, and
also depends on the state of the digestive tract, liver and kidneys.
One of the important regulator of calcium-phosphorus metabolism
is parathyroid hormone (PG). The production of this hormone by
parathyroid glands increases with hypocalcemia, and, especially,
with a decrease in plasma and extracellular fluid concentrations of
ionized calcium. Main target organs for parathyroid hormone are
the kidneys, bones and to a lesser extent gastrointestinal tract.
The effect of parathyroid hormone on the kidneys is manifested by
an increase in calcium reabsorption and magnesium. At the same
time, the reabsorption of phosphorus is reduced, which leads to
hyperphosphaturia and hypophosphatemia. It is also believed that
parathyroid hormone increases the ability of the formation of
calcitriol in the kidneys, thereby enhancing the absorption calcium
in the intestine.
In bone tissue, under the influence of parathyroid hormone, bone
apatite calcium goes into soluble form, thanks to which it is
mobilized and released into the bloodstream, which accompanied
by the development of osteomalacia and even osteoporosis. In this
way, parathyroid hormone is the main calcium-saving hormone. He
carries rapid regulation of calcium homeostasis, constant
regulation of calcium metabolism - function of vitamin D and its
metabolites. PG production is stimulated hypocalcemia, with a high
level of calcium in the blood, its production decreases.
The second regulator of calcium metabolism is calcitonin (CT) - a
hormone produced by the C-cells of the parafollicular thyroid
apparatus. By action on calcium homeostasis, he is an antagonist
of parathyroid hormone. Its secretion increases with increasing
levels of calcium in the blood and decreases with decreasing. A
diet high in calcium also stimulates secretion of calcitonin. This
effect is mediated by glucagon, which is thus biochemical activator
of the production of CT. Calcitonin protects the body from
hypercalcemic conditions, reduces the number and activity of
osteoclasts, reducing bone resorption, increases calcium
deposition in the bone, preventing development of osteomalacia
and osteoporosis, activates its excretion in the urine.
Task №48
At the examination, the dentist diagnosed the patient with
periodontal disease in the initial stage. During examination, an
increased concentration of calcium, osteocalcin protein,
parathyroid hormone was found in the patient's blood. The
phosphate content is below normal. What disease can correspond
to these data?
1. Describe the effect on the target tissue of a hormone, the
content of which is increased in the patient's blood;
2. Explain the structure of osteocalcin protein and its function in
bone tissue;
3. Name other specific proteins of bone tissue, describe the
features of their structure;
4. Specify other markers of bone metabolism, the content of
which should be increased in the blood and urine of the patient.
The data obtained during the examination indicate osteoporosis
due to hyperproduction of parathyroid hormone
(hyperparathyroidism).
Osteoporosis (OP) is a systemic skeletal disease characterized by
a decrease in bone mass and impaired microarchitecture of bone
tissue, resulting in bone fragility leading to an increase in the
frequency of fractures.
1. Parathyroid hormone - a peptide of 84 amino acids. It is
excreted by the parathyroid glands with a decrease in calcium in
the blood.
Target tissues of parathyroid hormone:
 bone tissue
 kidneys
 small intestine mucosa
Effect on bone tissue: in bone tissue there are 3 types of cells:
osteoblasts, osteocytes and osteoclasts. Under the influence of
parathyroid hormone, the activity of osteoclasts and osteocytes is
stimulated. Due to the increased disintegration (resorption) of the
organic basis of bone tissue, and then there is demineralization.
Collagen, breaks down to individual amino acids, this leads to the
release of hydroxyapatite molecules from the bond with collagen.
Hydroxyapatites break down to Ca and P0 , which enter the
2+
4
3-
bloodstream, and hypercalcemia occurs. The increase in blood
phosphate does not occur, because they are excreted with urine.
Effect on kidneys : under the influence of parathyroid hormone in
the renal tubules, reabsorption (reabsorption) of calcium and
magnesium from primary urine into the blood increases. Excretion
of phosphates, potassium and bicarbonates with urine increases,
and the excretion of ammonium, protons and magnesium is
reduced.
Effect on intestinal mucosa: parathyroid hormone enhances
absorption of Ca from the intestine to the blood.
2+
2. Osteocalcin (bone-Gla-protein) - the main non-collagen

protein of the extracellular matrix of bones, synthesized and
secreted predominantly by osteoblasts.
The structure of osteocalcin is represented by a 49 amino acid
sequence, with 3 γ-carboxyglutamic acid residues (-Gla). The
biological activity of osteocalcin is dependent on carboxylation with
a vitamin-K dependent γ-glutamyl carboxylase enzyme.
The residues of γ-carboxyglutamic acid attaches 3 calcium ions
onto themselves and stack them into the structure of
hydroxyapatite crystals, the main constituent bone tissue providing
its mineral density. By attaching Ca ions, osteocalcin reduces
2+
their concentration in the extracellular matrix, therefore calcium

binding to OH decreases, which participates in the formation of
crystallization centers, i.e. the bone does not undergo excessive
mineralization.
Expression of the osteocalcin gene is regulated by calcitriol, which
increases the transcriptional activity of the protein gene in
osteoblasts. With a decrease in the synthesis and secretion of
osteocalcin, an increase in bone mineralization is observed.
Osteocalcin is found only in bones and teeth, the increase in its
level in the blood indicates the rate of osteogenesis.
3.
Protein name Structural features

1. Osteonectin Glycophosphoprotein, able to bind Са 2+
2. Thrombospondin A protein consisting of three identical

subunits linked by disulfide bonds; binds
to cell surfaces and other bone tissue
proteins.
3. Osteopontin Glycophosphoprotein, containing N- and
O- linked oligosaccharides; participates in
cell adhesion.
4. Bone Adhesive glycoprotein containing up to
sialoprotein 50% carbohydrates.
5. Matrix Gla- Protein containing 5 residues of 7-
protein carboxyglutamic acid; able to bind to
hydroxyapatite.
6. Fibronectin Glycoprotein, consists of two identical
subunits connected by two disulfide
bonds; promotes adhesion between the
cell and the matrix.
4. In plasma:
 Tartrate-resistant acid phosphatase (TRAP).
 C-terminal telopeptide of type I collagen (ІСТР)
 N-terminal telopeptide of type I collagen (NTx)
 Bone sialoprotein (BSP)
In urine:
 Excretion of calcium with urine
 Hydroxyproline (Hyp)
 Galactosyl-hydroxylysine (Ghyl)
 Pyridinoline (Pyd)
 Deoxypyridinoline (Dpd)
 C-terminal telopeptide of type I collagen (ICTP)
 N-terminal telopeptide of type I collagen (NTx)
Task №49
To the dentist, a woman came with complaints of loosening of the
teeth of her teenage daughter. After the examination, the doctor
sent the patient to analyze the level of parathyroid hormone and
estrogen in the blood. Why, the change in the concentration of
these hormones, from the point of view of the doctor, could be the
cause of this phenomenon in a girl? ANSWER the question :
Why the concentration of parathyroid hormone and estrogen can
cause teeth loosening ?!
The stimulus for secretion of parathyroid hormone into the blood is

a decrease in the concentration of calcium cations in the blood.
The physiological effect of parathyroid hormone is to inhibit the
formation of bone tissue by influencing the osteoblast and
osteocyte population. Those, in turn, secrete Insulin-like growth
factor 1 and cytokines that stimulate the metabolism of
osteoclasts. Activated osteoclasts secrete alkaline phosphatase
and collagenase, which leads to the destruction of the bone matrix.
The effect of parathyroid hormone is an increase in calcium
concentration in the blood plasma and a decrease in the calcium
content in the bones (demineralization of the bone matrix), a
decrease in the phosphate content in the blood plasma.
Estrogens (female sex hormones) affect the metabolism in bones,
especially the protein basis of bone. Under the influence of
estrogen increases the concentration of calcium and phosphorus
in the blood, which contributes to the process of ossification.
Estrogen is involved in the formation of teeth, but its increased or
decreased level leads to a weakening of enamel.
Algorithm of the decision

1) indicate the metabolism of some tissues may be disrupted at the
girl;
2) explain the effects of parathyroid hormone and estrogen on
metabolism in this tissue;
3) Assume the level of any of the hormones will be normal, and
some below the norm in girls.
1) Metabolism of mineralized connective tissue (bone, enamel,
dentin, cement);
Mineralized tissues, which include bone tissue, dentin, cellular and
cell-free cement and tooth enamel, are characterized by a high
content of the mineral component, the main component of which
are phosphate calcium salts.
2) Parathyroid hormone - stimulates bone resorption, increasing

the activity of osteoclasts. Membrane receptors for parathyroid
hormone have only osteoblasts and osteocytes.
Estrogen acts on chromatin, causes expression of the
osteoprotegerin protein gene, which leads to a decrease in the rate
of formation of multi-core osteoclasts and slowing the process of
bone resorption.
The hormone in osteoblasts stimulates the synthesis of collagen
type I, alkaline phosphatase, osteonectin, and other organic
substances of the bone matrix. In adolescent girls with insufficient
estrogen production, there are changes in periodontal tissues and
impaired bone formation.
3) The girl's level of parathyroid hormone is likely to be normal,

and the level of estrogen is below normal.
Task №50
Fluorides are one of the most well-known anticarious agents.
They can enter the enamel with drinking water or directly on the
tooth surface.
when using fluoride toothpastes. Having information about high
demand for fluoride toothpastes, manufacturers of chewing gum
We also decided to include fluorides in our products. However, in
consultation with
dentists, they were forced to abandon the idea. Why dentists
banned fluoride from chewing gum? To answer the question
explain:
1) the mechanism of the anti-caries action of fluorides;
The amount of fluoride deposited in mineralized tissues directly
depends on its entry into the body from various sources, primarily
from drinking water.
The receipt of optimal doses of fluoride in the child’s body before
teething contributes to:
l increase the size of hydroxyapatite crystals;
l replacing hydroxyl groups (OH) in hydroxyapatite with fluorine
ions to form fluorapatite crystals;
l reducing carbonate content in enamel;
l increase the strength and reduce the solubility of enamel;
l Formation of deeper and wider fissures.
The mechanism of the anti-caries action of fluoride after teething: l
inhibits the process of demineralization and accelerates the
remineralization of enamel;
l impaired metabolism of cariogenic bacteria.
2) why using fluoride toothpastes is useful, and using

chewing gum containing fluoride is dangerous for the teeth;
Fluoride ions (fluorides) are necessary for the teeth: they inhibit the
vital activity of harmful bacteria and do not allow the products of
their vital activity to erode the tooth enamel. Thus, fluoride in
toothpaste prevents tooth decay. The damaged areas of the tooth
are remineralized due to the action of fluoride. It's all about
concentration. We clean the toothpaste and then wash it with
water, so we give a temporary effect.
Chewing gum can be chewed for no more than 5 minutes and only
after eating. As we all know, people usually chew gum for a long
time. And the use of chewing gum containing fluoride, with long-
term use can bring fluorosis (excess fluoride in the body). There is
a change in the color of the tooth enamel and the appearance of
white, yellow, brown spots and points on the teeth; the sensitivity
of the tooth enamel to cold, hot and salty food is lost; gradual
erasure of tooth enamel and dentin exposure, erosion and tooth
damage occurs. If the disease is very advanced, there may be
damage to the bone tissue, nervous system, muscles.
3) what consequences could the uncontrolled use of such

products by children and adolescents.
products by children and adolescents.
The entry of large amounts of fluoride into the body of children can
lead to enamel and dentin hypoplasia. Excess fluorine compresses
the surface layer of tooth enamel, limiting the intake of calcium and
phosphorus and thereby preventing the mineralization process.
Enamel children are most sensitive to the effects of toxic doses of
fluoride in the period from one to three years after the eruption of a
tooth, because the cut tooth is low mineralized, and an excess of
fluorine further limits the process of its mineralization. Therefore,
during this period, it is necessary to apply toothpastes with low
fluorine content or without it.
Task №51
Task №52
According to scientists, the use of hisstatins may become a new
trend in the prevention and treatment of periodontal diseases.
Explain why these proteins attracted the attention of scientists
developing new methods of treatment. For this:
1) name the unique proteins of the salivary glands and indicate the
features of their structure;
2) describe the functions of these proteins and suppose which of
them has aroused the interest of scientists.
1) Histatins (histidine-rich proteins). From the secrets of the human
parotid and submandibular salivary glands, a family of major oligo-
and polypeptides distinguished by a high content of histidine has
been isolated. The study of the primary structure of histatin
showed that they consist of 7-38 amino acid residues and have a
greater degree of similarity between themselves. The hisstatin
family is represented by 12 peptides of different molecular weights.
Individual peptides of this family are believed to form in reactions
of limited proteolysis, either in secretory vesicles or during the
passage of proteins through the glandular ducts.
2) - by binding with hydroxyapatite crystals enamel histatites are

involved in the formation of the pellicle of the tooth;
- interacting with phosphates, they inhibit the growth of crystals of
hydroxyapatites in saliva;
- inactivate proteases secreted by oral microorganisms;
- their bactericidal property is based on the ability to form a spiral
structure in the bacterial cell membrane, which increases its
permeability and causes the death of microorganisms. This
protective function is most actively manifested in histatins against
C. albicans. This function attracted the attention of scientists.
Task №53
Tannin contained in plant-based products such as quince,
persimmon, tea forms covalent bonds with the glycoproteins of
saliva, epithelium of the oral cavity and causes their denaturation.
Protein-tannin complexes are adsorbed on the surface of pellicle
and accelerate the formation of plaque. The body's response to the
intake of tannins is the fascination with the content in the saliva of
proteins rich in proline. Explain this phenomenon. For this:
1) indicate the functions of these proteins and describe their
structure;
2) What secrets of the salivary glands contain the main amount of
proteins rich in proline?
1)PRP (proline rich proteins) perform several functions in the oral
cavity. First of all, they are easily adsorbed on the enamel surface
and are components of the acquired pellicle of the tooth. Acid
BBPs that are part of the pellicle of the tooth bind to the protein
sterin and prevent it from interacting with hydroxyapatite at acidic
pH values. Thus, acidic PRPs delay the demineralization of tooth
enamel and inhibit excessive sedimentation of minerals, i.e.
maintain a constant amount of calcium and phosphorus in the
enamel of the tooth. Acidic and glycosylated PRPs are also able to
bind certain microorganisms and thus participate in the formation
of microbial colonies in plaque. Glycosylated PRPs are involved in
the wetting of the food lump. It is believed that the main PRPs play
a role in the binding of tannins in food and thereby protect the oral
mucosa from their damaging effects, as well as impart visco-elastic
properties to saliva.
of plaque.
Basic PRPs are secreted only by the parotid salivary glands,
accounting for up to 23% of the total protein in their secretion.
They bind C. albicans, which can affect the colonization of
surfaces in the oral cavity by these microorganisms and,
moreover, are endowed with antiviral activity.
Basic PRPs protect the oral mucosa from tannins. Currently, more
than 4,000 tannins are known - bioflavonoids, many of which have
one or more OH groups capable of binding proteins (tan proteins).
In animal experiments, it has been shown that tannins are able to
induce the synthesis of PRP.
2) The proline rich proteins are mainly secreted by the secretion of

the parotid salivary glands. They are encoded by various genes. In
these proteins, proline, glycine and glutamine make up from 70%
to 88% of all amino acid residues. In addition to saliva, they were
also found in the lacrimal fluid and respiratory tract.
Task №54
In the experiment on tissue sections, it was shown that, when the
suspension of dental plaque was injected into the incubation
medium, the cells and the intercellular matrix of the sections were
damaged. Explain the cytotoxic effect of the plaque suspension.
For this:
1) name low-molecular substances and proteins synthesized by
microorganisms of dental plaque;
2) describe the mechanism of the damaging action, provide
diagrams of each of these substances on the cells and
components of the intercellular matrix of tissue sections
1-2)
1. Ammonia (NH3) is formed by microorganisms during the
catabolism of amino acids, as well as from urea under the action of
bacterial urease. NH3 passes into the gingival epithelium, where,
by binding a proton, it is converted into NH4 +, as a result of which
the pH rises in these cells. Maintaining the optimum pH in the cells
provides two reactions: the synthesis of glutamine and the
reductive amination of α - ketoglutarate. An increase in the rate of
these reactions leads to a decrease in the content of NADH, α-
ketoglutarate and impaired energy metabolism (DIC) in epithelial
cells.
Amination reaction of α - ketoglutarate catalyzed by glutamate

dehydrogenase:
α-Ketoglutarate + NADH + H + + NH3 → Glutamate + NAD + +
H2O
2. Low molecular weight fatty acids are synthesized by
microorganisms from glucose, pass through the cell and
mitochondrial membranes of epithelial cells and separate oxidation
and phosphorylation. A decrease in the ATP / ADP ratio disrupts
the processes of synthesis of substances necessary for the cell.
3. Indole is the product of the conversion of tryptophan by
enzymes of microorganisms, mainly Porphyromonasgingivalis.
Indole enters the gingival fluid and from there enters the epithelial
cells. It is a xenobiotic for cells, so its accumulation violates their
metabolism.
4. Hydrogen sulfide (H2S) is formed by microorganisms in the
course of catabolism of sulfur-containing amino acids. H2S is an
inhibitor of the cytochrome oxidase enzyme CPE and inhibits
energy metabolism in epithelial cells.
5. Microorganisms of periodontal pockets produce amines, for
example, hydroxylamine (NH2OH), which is a strong oxidizing
agent: NH2OH + 2e → NH3 + O-
The source of electrons can be any heme- or Fe2 + -containing

proteins: cytochrome ETC(electron transport chain), antioxidant
protection and other cell enzymes. Hydroxylamine not only violates
oxidative phosphorylation in mitochondria, but also causes
damage to the cell membranes by active radicals, as it activates
lipid peroxidation.
6. Inflammatory and toxic effects on cells have enzymes produced
by microorganisms. They easily penetrate into the gum tissue with
the help of bacterial hyaluronidase (proliferation factor or
aggression enzyme), which causes hydrolysis of the main GAG of
the extracellular matrix. The pathogenic effect of hyaluronidase is
enhanced by the joint action of the enzyme collagenase on the
extracellular matrix of tissue. Bacterial proteases have the most
aggressive effect on periodontal tissues. Collagenase, hydrolyzing
collagen, causes the destruction of the protein matrix. Elastase,
which is produced by bacteria, is capable of destroying elastin (for
example, the vascular wall).
Bacterial neuraminidase, splitting off the remains of N-
acetylneuraminic acid, changes the structure of cell membrane
oligosaccharides. This stimulates the production of antibodies to
damaged cells, increases the cytotoxic effect of antibodies,
proteins of the complement system. The activation of the
complement system is accompanied by the formation of peptides
that stimulate the migration of leukocytes to the area of localization
of damaged cells and their destruction.
Pathogenic properties are bacterial phospholipase C and DNA

hydrolase.
Phospholipase C hydrolyzes phosphatidylcholine (lecithin) of cell
membranes, as a result of which their permeability increases,
metabolism is disturbed, and cells die. DNAse cleaves DNA.
Task №55
It is known that the use of Coca-Cola, forfeits, beer, containing in
large quantities of sucrose and maltose, contributes to the
development of caries. Explain the causes of caries when using
these drinks. For this:
1) indicate the pH of the saliva is normal; explain how the sucrose
and maltose contained in these drinks can cause a change in pH;
2) describe the structure of the compound that microorganisms
can synthesize from sucrose, and its role in the formation of
plaque;
3) name the possible substitution reactions occurring in
hydroxyapatite enamel, while reducing the pH of saliva and explain
the possible consequences.
1) Normal saliva pH is in the range of 6.8–7.5. It was established
that the acidity of saliva depends on the rate of salivation and at
large values it can reach a pH of 7.8.
In the presence of carbohydrate residues of food, and especially
sucrose, their decomposition occurs very quickly, in the form of a
metabolic explosion, accompanied by the formation of a large
amount of organic acids. The formed acids, in case of their
insufficient neutralization, locally reduce the pH of the dental
plaque to a critical level (below 5.0), dissolve the pellicle and
cause focal demineralization of enamel - the first stage of caries.
2) Microbes of plaque contain highly active enzymes that break
down carbohydrate residues of food, especially intensively -
sucrose. Food sucrose is selectively absorbed by dental plaque
and is exposed to the enzyme plaque enzyme microbial origin. At
the same time, fructose and glucose are formed, which are
deposited in the composition of dental plaque in the form of
specific fructan-levan and glucan-dextran polysaccharides,
increasing the mass of dental plaque and creating a nutrient
medium for microorganisms. Glucan and fructan ultimately
contribute to the formation of dental plaque and its attachment to
the enamel surface. Microbes of bacterial plaque also contain a
complete set of highly active enzymes of glucose catabolism,
especially its anaerobic decay. In the process of glucose
decomposition various organic acids are formed, among which
lactate predominates.
3) With a decrease in the remineralizing potential of saliva due to a
decrease in the concentration of phosphorus-calcium salts, a
violation of the micellar structure of saliva, a shift in pH below 6.2,
the acid dissolution of the enamel progresses. Hydrogen ions
penetrate through the inter-prism spaces, first into the subsurface
enamel layer, partially dissolving the apatite crystals and
expanding the interprismatic spaces. The predominance of acid-
resistant apatites in the surface layer of enamel is a limiting factor
in the emergence and progression of the primary focus of enamel
demineralization. The loss of calcium ions leads to a decrease in
the Ca / P ratio. The demineralization zone first spreads parallel to
the tooth surface and then in the form of a cone deep into the
enamel. At the same time, the permeability of enamel increases,
the share of microspaces of enamel gradually increases,
microorganisms and organic substances, including proteins from
the oral fluid, penetrate into them. Therapeutic measures at this
stage should be aimed at eliminating the causes of
demineralization on the background of remineralizing therapy.
Further progression of the process leads to a violation of the
enamel-dentin barrier of permeability, which opens up the
possibility of penetration of irritating effects on the odontoblasts
and the pulp. The response of the odontoblasts is the obliteration
of the dentinal tubules and the deposition of secondary dentin. The
most important pathogenetic moment of caries development at this
stage is the penetration of microbes into the deep layers of enamel
and dentin through the enamel-dentin boundary. Under the action
of microbial and leukocyte enzymes (proteases, hyaluronidase,
various glycosidases and other hydrolases), the matrix of
mineralization of enamel and dentin is split, resulting in the
development of caries becoming irreversible. It has been shown
that in the demineralization focus, up to 70% of matrix proteins are
cleaved. Remineralizing therapy at this stage of caries
development becomes ineffective and inappropriate. Bacterial
seeding of naked dentin is a leading factor in the further
progression of the pathological process, which can lead to the
development of caries of the tooth root.
Thus, at the first stage of caries development, the balance
between remineralization and enamel demineralization shifts
towards demineralization due to acid dissolution of enamel
apatites.
Task №56
Task №57
Recently, dentists have noted the emergence of a new disease - a
chewing disease. Due to improper use of chewing gum in patients
with atrophy of the salivary glands. How will saliva secretion
change with this disease? To answer the question:
Xerostomia - is dry mouth. It is marked by a decrease in salivation

due to salivary gland damage.
1) list the main functions of saliva;
Digestive. Saliva wets the incoming food, contributes to the
formation of food lump, swallowing. Dissolving food substances
contributes to the taste analysis of food substances. Amylase and
maltase saliva hydrolyze starch to monosaccharides.
Trophic. Saliva is an external environment for teeth, the mineral
composition of which affects the state of enamel. Ca, P, F, coming
from saliva, contribute to the compaction of enamel and increase
its resistance. In the absence of saliva, teeth are particularly
vigorously affected by caries.
Protective. Due to the presence of lysozyme and proteolytic
enzymes of trypsin-like action, saliva has antibacterial properties.
The presence of coagulation and fibrinolytic factors in it ensures
good and rapid healing of the oral mucosa when it is damaged.
Salivation is associated with the regulation of water and electrolyte
balance of body fluids. When salivation decreases, there is a
feeling of thirst, which in turn stimulates fluid intake.
Excretory. In violation of the excretory function of the kidneys in
the saliva increases the content of excreta. These can be salts of
iodine, mercury, lead, arsenic, metabolic products - uric acid,
ammonia, urea, creatinine. Exogenous substances introduced into
the body can be excreted with saliva, for example, drugs:
antibiotics, vitamins, salicylates, etc. Certain hormones, for
example, androgens, estrogens, gluco-and mineralocorticoids,
thyroxin and their metabolites can be expelled from saliva.
As well as in humans, saliva is necessary for the implementation of
speech function. It provides hydration of the oral mucosa for
adequate formation of sounds.
2) indicate how a change in the secretion of saliva will affect the
state of the enamel of the teeth and oral mucosa;
Saliva, being the main source of calcium and phosphorus for tooth
enamel, influences the formation of tooth resistance to caries.
With a decrease in the secretion of saliva in the oral cavity, there
are numerous adverse manifestations: a feeling of dryness,
difficulty in swallowing solid foods and talking. And also can lead to
an increase in the intensity of caries.
On average, 1–2.5 l of saliva is secreted per day.
saliva pH ranges from 6.4 to 7.8
Fluctuations in the pH of saliva depend on the hygienic condition of
the oral cavity, the nature of the food, and the rate of secretion.
With a low rate of secretion, the pH of the saliva shifts to the acidic
side, which contributes to the development of caries (pH <5), while
stimulating salivation to the alkaline one.
A decrease in pH below 5.0 can lead to enamel demineralization.
However, such a strong acidification of the saliva in the mouth is
rarely due to the functioning of the buffer systems. Local
acidification occurs more frequently in the area of the formation of
soft plaque. During demineralization:
 enamel becomes rough;
 white cretaceous spots appear (меловидные пятна);
 light spots darken, turn brown;
 Enamel gets a "porous" look(пористый вид).
Increasing the pH of saliva relative to the norm (alkalization-
защелачивание) leads to an increase in the rate of mineralization
of enamel. However, this increases the rate of
deposition(отложения) of tartar-зубной камень.
3) explain what unpleasant symptoms led these patients to the

dentists.
The patient is worried about burning and itching(зуд), taste
disturbance, difficulty in talking, swallowing food (especially dry). In
connection with this, the need for a liquid rises, especially during
meals, and there is a need for frequent use of agents that maintain
the humidity of the oral cavity

Biochemistry

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Biochemistry

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What are the main functions of saliva?

What are the main functions of saliva?

How does a change in saliva secretion affect the enamel and oral mucosa?

How does a change in saliva secretion affect the enamel and oral mucosa?

Biochemistry Final (Eng Version)

Algorithm of the decision:

Heat (high temperature) causes protein denaturation, which

0-60° C - reversible denaturation,

1. Decrease or complete absence of liver enzyme

Isoniazid - violates the formation of pyridoxal phosphate coenzyme

Nicotinamide can be formed from tryptophan, which is an

1.What kind of exchange is impaired in a child. What is the name

1) Due to hypervitaminosis, an earlier ossification of the skull

2) . Vitamin D is formed from sterols during their ultraviolet

Ergocalciferol and cholecalciferol in the liver, by oxidation, form 25-

3) Vitamin D maintains the level of inorganic phosphorus and

Algorithm of the decision :

1)Carbohydrate metabolism is impaired (aerobic decomposition of

OH group of hydroxyproline, forming H-O bonds between the

3. Vitamin K1 (phylloquinone) - regulates blood coagulation in the

Vitamin K is also needed to build the tissues of the heart and

1. Hydrolases enzymes catalyzing the decomposition of complex

3. Polyvalent protease inhibitor, has antiproteolytic, antifibrinolytic

2. What additional biochemical parameters should be assigned to

3. What indicator should be determined in a patient to establish

To clarify the activity of the atherosclerotic process, standard

b) Scheme of the respiratory complex (enzymatic

2. Lactose is a disaccharide that is not able to be absorbed

2) Acarbose inhibits the enzymes (glycosidic hydrolases)

2) Three enzymes are directly involved in glycogenolysis:

2) Write a glycogenolysis scheme and specify the amount of ATP

3) Indicate which hormone levels increase in blood under stress and

Decay of glucagon to glucose - 6- phosphate doesn't require energy.

3. Catecholamines - these hormones are characterized by speed

• Participate in the emulsification of fats in the intestines

1) Write a glucose catabolism to acetyl CoA.

3) Show schematically the path of fatty acid synthesis.

2) In the absence of enzymes involved in the synthesis of

Algorithm of the decision:

1) TRANSFER OF ACTIVATED FATTY ACIDS WITH A LONG

All the enzymes of B-oxidation of fatty acids are in the

Under the action of carnitine-acyltransferase 1, fatty acid joins the

Acyl-Scoa + Carnitine = Acylcarnitine + NScoA

3) Formed by the condensation of two acetyl-CoA molecules,

2. The role of SALTIC ACID:

Algorithm of the decision:

2) Transamination is a reversible process of transferring an amino

3) Indicate which enzymes will increase in the blood of patients in

Algorithm of the decision:

3) Enzymodiagnosis consists in making a diagnosis of a disease

TSH and thyroliberin.

3. Because of the decrease in iodine intake from food, iodine-

Mechanism of action: Almost all of the T hormones turn into T ,

because of this, talking about the effect of this hormone in normal

where they turn into T , the active part of thyroid hormone.

c) Total and free T (triiodothyronine)

Mechanism of action: 2nd through cGMP

In the blood test, the level of T is also expected to be higher than

· Releases hormones from thyroglobulin;