Кузнецова Ольга Матвеевна


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 Topic 1

1.      Amino acids: their structure and properties. Classification of the amino acids.

2.      Essential and nonessential amino acids.

3.       Polypeptide chain.

4.       The ways of natural peptides synthesis.

5.       Examples of natural peptides: oxytocin, vasopressin, angiotensin, glutathione.

6.       Structural features of the peptides, providing their resistance to proteolysis.

7.       Amino acid composition of proteins. Color reactions of proteins.

8.      Levels of protein structure: primary, secondary, tertiary and quaternary structure.

9.      Relationship between the protein structure and biological function. The domain structure of proteins.

10.  Protein modification after the ribosomal synthesis (post-translational modification of  proteins).

11.  Folding of protein molecules. Role of chaperones. Protein misfolding.

12.  Physico-chemical properties of proteins. The isoelectric point of the protein solutions.

13.  Functions of proteins in the body.

14.  Methods of protein separation and purification: dialysis, fractionation, electrophoresis, chromatography (gel-filtration, ion-exchange chromatography, affinity chromatography).

Topic 2

1.      Classification of the complex proteins (examples)

2.      Nucleoproteins.The biological role. The chemical composition of nucleoprotein.

3.      Chromoproteins. The biological role. Structure of hemoglobin. Hemoglobinopathies and thalassemias. Cooperative binding of oxygen. Allosteric regulation.

4.      Phosphoproteins. Biological role. Character of chemical bonds with phosphoric acid.

5.      Chemical structure of nucleic acids. Primary, secondary and tertiary structure of DNA.

6.      Ribosomal, information and transport RNAs. Their structure, distribution and biological role.

7.      Biological catalysts. Ribozymes. Enzymes.

8.      The concept of the coenzyme. Coenzymes and vitamins.

9.      Active sites of enzymes (catalytic and regulatory centers). Allosteric effectors. Activators and inhibitors of enzymes.

10.  General properties of enzymes: thermolability, pH-dependence, the specificity of action. The concept of the rate of enzymatic reaction. Units of enzyme activity.

11.  Relationship between the substrate concentration and the rate of enzymatic reactions. The concept of the Michaelis constant.

12.  Types of enzyme inhibition: competitive, noncompetitive inhibition and uncompetitive. Lineweaver-Burk double-reciprocal plot.

13.  Isoenzymes and their significance for medicine.

14.  Classification of enzymes. Characteristic of each class of enzymes (examples).

15.  Intracellular regulation of enzyme activity.

Topic 3

1.      The concept of avitaminosis, hypo- and hypervitaminosis as diseases associated with dysfunction of the enzyme systems.

2.      Vitamins of group A. The structure and properties. The biological role. Food sources of vitamin A. Absorption in the intestine. Provitamins. Hypo- and hypervitaminosis. The daily requirement.

3.      Vitamins of group D. Structure and properties. Provitamins, ergosterol, 7-dehydrocholesterol. Dietary sources. The biological role. Hypo- and hypervitaminosis. The daily requirement. Clinical application.

4.      Vitamins of group E. Structure and properties. Hypovitaminosis. Dietary sources. Clinical application.

5.      Vitamins of group K. Structure and biological role. Clinical application.

6.      Vitamin B1. The structure and properties. Coenzyme form. Role in metabolism. Hypo- and hypervitaminosis. Dietary sources. The daily requirement. Clinical application.

7.      Vitamin B2. The structure and properties. Coenzyme forms. Role in metabolism. Dietary sources. The daily requirement.

8.      Vitamin B6. The structure and properties. Coenzyme forms. Hypovitaminosis. Dietary sources. The daily requirement.

9.      Vitamin B12. The chemical composition. Role in metabolism. Dietary sources. An absorption of B12. Clinical application.

10.  Vitamin C. Structure and properties. The biological role. Hypovitaminosis. Clinical application. The daily requirement.

11.  Biotin. The structure and properties. Hypovitaminosis. Dietary sources.

12.  Vitamin PP. Structure. Coenzyme forms. Hypo- and avitaminosis. Dietary sources. Role in metabolism. The daily requirement.

13.  Folic acid. Structure. Distribution in nature. Participation in the construction of coenzymes. Hypo- and avitaminosis.

14.  Vitamin B3. Structure. The biological role. The daily requirement.

15.  Chemistry of the lipids. The structure, classification, biological role, transport in the body.

16.  Glycerophospholipids and sphingolipids. Structure and biological role.

17.  The biological role of sterols. The chemical structure of cholesterol.

18.  Chemistry of fatty acids. Structure and biological role.

19.  General presentation of hormones. Hierarchy of hormones.

20.  The role of hormones in metabolism regulation. Mechanisms of hormonal signal transduction. Examples of hormonal signal transduction by protein receptors. The notion of G-proteins and second messengers. The intracellular and intranuclear receptors. Regulation of transcription.

21.  The hormones of the adrenal medulla. Their synthesis and breakdown. Mechanism of action. Role in the regulation of metabolism.

22.  Thyroid hormones. Their structure and formation in the body. Hypo- and hyperthyroidism.

23.  Pancreatic Hormones. Their chemical nature and the effect on metabolism. Insulin and glucagon.

24.  Hormones of steroid nature. Their structure and mechanism of action. Male and female sex hormones.

25.  The hormones of the adrenal cortex. The chemical nature and the effect on metabolism. Mechanism of action.

26.  The anterior pituitary hormones. The chemical structure of their biological effects. Hypothalamic hormones. Structure and biological role.

Topic 4

1.      General principles of energy and metabolism. Catabolism and anabolism are the basic metabolic processes. Role of NADPH (H +) and ATP.

2.      Monosaccharides, oligosaccharides. The most important representatives of monosaccharides and oligosaccharides of the animal organism. Chemical structure, biological role.

3.      Polysaccharides. Glycogen, its structure and properties. How Glycogen Is Produced and Degraded How does the breakdown of glycogen take place? How is glycogen formed from glucose? How is glycogen metabolism controlled?

4.      Anaerobic breakdown of carbohydrates, its biological significance. Energy effect. Substrate level phosphorylation.

5.      Glycolysis. Regulation. Energy effect.

6.      Gluconeogenesis. Energetic effect of the process. Regulation.

7.      Oxidative decarboxylation of pyruvic acid. Coenzymes and enzymes involved in this process.

8.      The citric acid cycle. Its biological significance. Regulation.

9.      Links between TCA cycle and biological oxidation.

10.  The Role of Electron Transport in Metabolism. Oxidative phosphorylation. Peter Mitchell and Chemiosmotic theory. ATP synthesis.

11.  Pentose phosphate pathway of glucose oxidation in tissues and its biological role.

12.  Mechanisms of regulation of blood glucose. Hypoglycemia and hyperglycemia. Diabetes. Diagnostic value of sugar curves.

13.  Possible ways of glucose-6-phosphate conversions in the liver.

Topic 5

1.      Peculiarities of absorption and transport of lipids.

2.      Degradation and synthesis of triacylglycerols.

3.      Oxidation of glycerol. 

4.      b-oxidation of fatty acid in mitochondria

5.      Biosynthesis of fatty acids and phospholipids in different tissues.

6.      Acetone bodies.

7.      Biosynthesis of cholesterol

8.      Links between lipid and carbohydrate metabolism. Central role of CoA in lipid metabolism. Regulation and pathology of lipid metabolism. Intracellular lipids and blood serum lipids.

9.      Microsomal oxidation of lipids. Role of cytochrome P450 in xenobiotic detoxification. Reactive oxygen species

Topic 6

1.      Problem of nitrogen nutrition. Essential and nonessential amino acids.

2.      Digestion of proteins in gastrointestinal system. Absorption and active transport of amino acids. Protein purification in the intestine (indole, skatole, phenol, cresol)

3.      Pathways of amino acid metabolism. Deamination (oxidative and non-oxidative) and transamination of amino acids. Role of the coenzymes in these reactions.

4.      Diagnostic significance of the aminotransferases in the blood

5.      The fate of α-keto acids. Glucogenic and ketogenic amino acids.

6.      Synthesis and degradation of biogenic amines and their biological role. MAO

7.      Notion on hydroxylation and methylation reaction. (Examples)

8.      The ammonia detoxification pathways. Urea synthesis in the liver.

9.      Metabolism of individual amino acids:

a)    Gly, Ser,

b)    Cys, Met,

c)    Arg,

d)   Glu, Asp,

e)    Phe, Tyr, Trp

10.  Biosynthesis of creatine phosphate and its physiological role.

11.  Regulation and pathology of amino acids metabolism.

Topic 7

1.      Sources of purine nucleus of atoms. Biosynthesis of AMP and GMP from inosinic acid.

2.      The degradation of purine nucleotides. Hyperuricemia and gout.

3.      Basic synthesis reaction of the pyrimidine nucleotides.

4.      The degradation of the pyrimidine nucleotides.

5.      The biosynthesis of nucleic acids.

6.      The biosynthesis of heme and its degradation. Determination of direct and indirect bilirubin in the blood serum.

7.      Protein biosynthesis. The main components of the protein synthesis system. Post-translational modification of the  proteins.

8.      Integration of the carbohydrate, lipids and proteins metabolism and its regulation.

9.      Examples of enzymes in the medicine. (LDH, ALT, AST, Alkaline phosphatase, creatine kinase and other)

10.  Abnormal urine components.

11.  Basic nitrogen-containing inorganic components and urine.

12.  The main chemical components of human serum.



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