BIOCHEMISTRY DEPARTMENT

Self-preparing questions for the examination for 2002-2003

Protein structure, functions and assay

1. Subject of biochemistry. Biochemistry importance for medicine. The greatest discoveries achieved in biochemistry in the XX th

century.2. Peculiarities of the alive matter. Levels and methods of its study.3. Protein primary structure. The peptide bond. Genetic changes of

amino acids sequence. Hereditary proteinopathies - sickle-cell anemia etc.

4. Methods for the determination of the amino acid sequence of proteins.

5. Secondary and tertiary structures of proteins. Covalent and non-covalent bonds specific for them. Conformation – function correlation’s.

6. Quaternary structure of proteins. Co-operative movement of protomers (on the example of hemoglobin). Protein folding.

7. Protein conformation. Bond that stabilized proteins. Conformational changes correlated to protein activity. Notion of “domain”.

8. Methods for the determination of the secondary, tertiary and quaternary structures of protein.

9. Protein's solubility. Factors that influence it. Protein colloidal solution. Properties and factors of stability.

10. Amphoteric and electro-chemical properties of proteins. ISO-electric state and point.

11. Proteins molecular mass. Methods for it determination.12. Protein’s classification. Simple and conjugated proteins. Brief

characteristic.13. Protein's classification. Simple proteins: histones, albumin and

globulin – physicochemical properties and functions.14. Protein's classification. Conjugated proteins: phospho-, glico- and

lipoproteins – brief characteristics.15. Protein's classification. Conjugated proteins: nucleo-, cromo- and

metaloproteins – brief characteristics.16. Collagen – peculiarities of amino acid composition, structure and

properties.17. Ca2+ - binding proteins – calmodulin, Ca2+-ATP-ase etc –

peculiarities of amino acid composition and structure.18. Immunoglobulins – peculiarities of the structure.19. Functions of proteins. Selective interaction with the ligands.

Ligand's recognition.20. Chemical nature and function of the enzymes. Similarities and

differences with non-biological catalysts.21. Function of the enzyme22. Enzyme structure. Active and allosteric sites-nature and role.

Notions of substrate and allosteric modulator (effector).23. Simple and conjugated enzymes. Notions of cofactor, coenzyme

and prosthetic group.24. Water-soluble vitamins as coenzymes. Structure and metabolic

function of vit. B1, B2, B6, PP, C, biotin, folic and pantothenic acids.25. Fat-soluble vitamins as coenzymes. Structure and metabolic

function of vit. A, E, D and K.26. Provitamins and antivitamins – notion, examples and role.

Hypovitaminose and hypervitaminose – notions, repercussions and examples.

27. Enzymes mechanism of action.28. Enzyme kinetics. Influence of temperature, pH, substrate and

enzyme concentrations, on the reaction rate29. Regulation of enzyme activity. Inhibition and activation types –

brief characteristic.30. Competitive, noncompetitive and allosteric inhibition. Medical

utility of competitive inhibition.31. Enzymes activity regulation by phosphorylation and

dephosphorylation – role, examples.32. Enzyme activation by partial – proteolysis, quaternary auto-folding

and allosteric mechanism.33. Enzymes specificity – types, brief characteristics and examples.

Fisher's and Coshland's theories.34. Genetic diversity of enzymes. ISO-enzymes. Examples. Medical

utility.35. Polyenzyme complexes – types of organization and examples.36. Enzyme's classification. Brief characteristic of each class.37. Methods of enzyme separation and purification. Affinity

chromatography.38. Enzyme's activity assay. Units of enzyme activity39. The use of enzyme assay in diagnosis. Enzyme of diagnostic

interest, examples.40. Biochemical adaptation. Enzyme induction and repression.

Inductive and constitutive enzymes.

Nucleic acids

1. Nucleic acids – types, function and cell distribution.2. Components of nucleic acids – nitrogenous bases, sugars

and phosphate. Major and minor nitrogenous bases.3. Nucleosides, nucleotides: structure, nomenclature and

functions. Cyclic nucleotides: cAMP, cGMP – structure and role.

4. DNA – primary and secondary structures. Chargaff's, Watson's a Crick’s conceptions about DNA composition and structure.

5. DNA – tertiary structure. Nucleosomes. Chromatin6. Conformation of the DNA double helix.7. Denaturation, renaturation and hybridization of DNA.

Practical utility.8. Structure of RNA – primary, secondary and tertiary.9. tRNA – structure and role in protein biosynthesis10. mRNA – structure and role in protein biosynthesis11. rRNA – structure and role in protein biosynthesis12. Ribosome – structures and functions. Polysomes or

polyribosomes13. DNA – biosynthesis: substrates, enzymes, mechanism14. Replication – characteristic of the initiation stage

(formation of replication forks).15. Replication – biosynthesis of the leading strand and lagging

strand.16. Repair of DNA – enzymes, mechanism and importance.17. RNA biosynthesis or transcription – notion, structure of the

operon and transcription, role of each component.18. RNA biosynthesis – substrates, enzyme, mechanism and

stages.19. Post-transcriptional modification of RNA molecules20. RNA replication – mechanism and significance21. Inhibitors of nucleic acids biosynthesis – examples,

mechanism of action and medical utility.22. Protein biosynthesis or translation – stages and their brief

characteristic.23. Translation. Activation of amino acids. Aminoacyl – tRNA

synthetases – properties and functions. The adapter role of tRNA

24. Initiation stage of translation – composition of the initiation complex, the steps of its formation, protein factors that are involved and their role.

25. Characteristic of the elongation and termination stages of translation. Enzymes and protein factors that are involved

26. Post-translational modifications of protein molecules27. Inhibitors of protein synthesis. practical utility in medicine28. The central dogma of genetics. The genetic code –

characteristics and properties.29. Mutations. Physical and chemical mutagenes. Kinds of

mutations. Consequences of mutations. Genetic diseases – notion and examples

30. Regulation of gene expression in prokaryotes and eukaryotes. The operon model of Jacob and Monod. Positive and negative control of operons. Hormone involvement in gene expression regulation.

31. Reverse transcription: enzymes, mechanism and practical utility. Genetic engineering.

32. Incomplete DNA replication (Olovnikov's theory). Thelomere and thelomerase

33. Structure, function and modulators of thelomerase activity34. Mortality and eternity at cellular level. Thelomere – a

promising indicator of cancer cell eternity35. Write the structure of 5' – ATCG – 3' and 5' – CUGA – 3'.

Show the similarities and differences36. Which are the similarities and differences of DNA and

RNA biosynthesis?37. Enumerate all type of bonds that can be find in DNA

molecules.38. The greatest discoveries achieved in nucleic acid studies in

the XXth century. Scientist that made this discoveries.1. Histones – peculiarities of composition and physic-chemical

properties. DNA – histones association – bonds structure and

2. Microsomal electron transport chain: structure, functions and tissue location

39. Oxygen toxicity. Oxygen free radicals: representatives, functions of nucleosomes.

40. What are the differences in polynucleotide phosphorylase and DNA polymerize action?

Introduction to metabolism. Bioenergetics.

3. Metabolism. Definition. Functions. Catabolism and anabolism. Final common pathway of metabolism

4. Metabolic pathways: central and specific, cyclic and linear, amphibolic. Examples

5. Metabolism – methods of study.6. Stages of the catabolism and anabolism. The common pathway of

catabolism and anabolism, its role.7. Catabolism and anabolism – notion, functions and connections.8. High-energy phosphate compounds – structure, properties and

function. The ATP cycle. The ways of ATP biosynthesis and utilization. ATP as a universal energy carrier between catabolic and anabolic pathways.

9. Low – energy, high – energy and super high-energy phosphate compounds – structure, role and correlation’s between them.

10. Energetic state of the cell. Indicia and role in metabolism regulation.

11. The fundamental thermodynamic concepts. Enthalpy, entropy and free energy – notions, their changes, correlation and standard state.

12. Free energy, standard free energy, standard free energy change of a reaction. Exergonic and endergonic reactions. Coupled reactions

13. Oxidation – reduction reactions. Oxidation – reduction (redox) potential. Standard redox potential and its correlation with standard free energy.

14. Oxidative decarboxylation of pyruvate: location, multienzyme complex, reactions, stoichiometry and control.

15. Oxidative decarboxylation of pyruvate – reactions, products and connection with tricarboxylic acid cycle.

16. Oxidative decarboxylation of pyruvate – reactions, products and connection with the respiratory chain.

17. Pyruvate dehydrogenase enzyme complex – enzymes and coenzymes. Structure and role of the vitamins in PDC.

18. Energetic output of complete oxidation of pyruvate.19. The tricarboxylic acid cycle (Krebs cycle) – functions, location and

reactions.20. The Krebs cycle – reactions and correlation with respiratory chain.21. The citric acid cycle – reactions, enzymes, their class and

modulators. Cycle regulation.22. Stoichiometry of the Krebs cycle. Anaplerotic reactions – role and

examples.23. Energetic output of the acetyl-CoA oxidation in tricarboxylic acid

cycle.24. Explain why Krebs cycle is an aerobic process?25. The substrate – level phosphorylation reaction of the Krebs cycle –

mechanism, enzyme and significance26. Mitochondria electron transport chain (ETC) – localization,

structure and functions.27. Sources of protons and electrons. Dehydrogenation reactions the

main energy sources in human cells. NAD- and FAD-linked dehydrogenases and their connection with the ETC.

28. The glicerol-3-phosphate and malate – aspartate shuttle systems – role, cell location, reactions, enzymes and connection with ETC.

29. Organization of the ETC. structure of its components. Their oxidized and reduced state.

30. Organization of the ETC. the respiratory chain complexes – composition, role and mechanism of action.

31. Mechanism of proton and electron transport in the ETC. energy change during the proton/electron transport and ATP formation

32. Redox potential and free energy changes in the ETC that can support ATP formation. Sites of phosphorylation The P/O ratio

33. Long, media and short ways of electron transport: sources of electrons point of entry to ETC and ATP formation.

34. Oxidative phosphorylation – coupling of phosphorylation to respiration. ATP – synthase – structure and function.

35. Mechanisms of oxidative phosphorylation – chemical, conformational and chemiosmotic coupling hypothesis

36. Inhibitors of electron transport, uncouples of oxidative phosphorylation and phosphorylation inhibitors – role, examples and consequences of their influencemechanism of formation and toxicity. Lipid peroxidation. Antioxidant system – enzymes and non-enzymatic compounds

37. Substrate – level phosphorylation – definition, examples and role38. Write down the structure of vitamins and vitamin-like compounds

from the ETC. What's their common property?

39. Describe the chemical structure of cytochromes. What's the peculiarity of cyt.a3? Its significance.

40. The mitochondria structure and properties. Translocation across the inner mitochondria membrane. Role of translocases and shuttle systems.

Chemical structure and metabolism of carbohydrates

1. Carbohydrates – definition, functions, classification and nomenclature

2. Structure and functions of mono-saccharides and their derivatives (sugar acids, phosphoric acid esters and amino sugars)

3. Structure and functions of disaccharide – maltose, sucrose and lactose.

4. Structure and functions of polysaccharides – amylose, amylopectin, starch, glycogen and cellulose

5. Glycoproteins and proteoglycanes – functions and structure of the oligosaccharide component

6. Glicozaminoglicanes: hialuronic acid, chondroitin – sulfates, heparin – functions and structure.

7. Digestion and absorption of carbohydrates. Diseases associated with digestion and absorption of carbohydrates – lactose intolerance.

8. Glycogen synthesis (glycogenesis) – role, major tissue sites, reactions, enzymes, coenzymes and regulation

9. Glycogen utilization (glycogenolysis) – role, reactions, enzymes and regulation.

10. Genetic defects in glycogen metabolism – Von Gierke's disease, Pompe's disease, Forbes - Cori's disease etc.

11. General description of glycolysis (Embden Meyerhof) – definition anaerobic and aerobic pathways, stages, role, stoichiometry.

12. The enzymatic reactions of glycolysis anaerobic pathways. Stoichiometry.

13. The aerobic pathway of glycolysis – partial reaction up to pyruvate, final products, stoichiometry.

14. Energetic output of anaerobic glycolysis. Lactate metabolism. The Cori cycle. Major tissue sites of anaerobic glycolysis. Lactic acidosis.

15. Energetic output of aerobic glycolysis. Mechanisms for translocation of H+/ē) from cytosol into mitochondria matrix: -glycerophosphate and malate-aspartate shuttle systems.

16. Glycolytic reactions of dehydrogenation. Their link with the ETC

17. Glycolytic reactions of substrate – level phosphorylation, their importance.

18. Regulation of glycolysis (enzymatic control).19. Gluconeogenesis – definition, functions, precursors, tissue

location, partial reactions, energetic expenses20. Gluconeogenesis from pyruvate – full description

(reactions, enzymes, regulation, stoichiometry)21. Gluconeogenesis from amino acids - substrates, reactions,

importance22. Gluconeogenesis from oxaloacetate – reactions, energetic

expenses, regulation23. Correlated regulation of glycolysis and gluconeogenesis24. Stoichiometry of anaerobic glycolysis and gluconeogenesis25. The glucose – lactate cycle (Cori) and glucose – alanin

cycle – description and biologic role.26. Control of the blood glucose concentration in health:

insulin, glucagon, and glucocorticoid influence.27. Blood glucose concentration in disease. Hypo-,

hyperglycemia and glucosuria. The glucose tolerance test28. The pentose phosphate pathway-tissue location, functions,

stages partial reactions of the first stage.29. The pentose phosphate pathway – partial reactions of

pentose formation, regulation30. The glucuronic acid pathway – functional significance,

reactions31. The metabolism of fructose in muscles.32. The metabolism of fructose in liver33. Hereditary disorders of fructose's metabolism34. The galactos metabolism. Hereditary disorders of

galactose's metabolism.35. The biosynthesis of lactose – pathway, control and

functional significance

36. Alcohol fermentation – reactions, energetic output, significance37. Diabetes mellitus – types metabolic disorders and consequences.38. Mechanism of hyperglycemia, glucosuria, ketonemia and ketonuria

in diabetes mellitus39. Biochemical mechanisms of diabetic coma.40. Energetic output of sucrose and lactose oxidation

Chemical structure and metabolism of lipids

1. Lipids – functions and classification and properties2. Triacylglycerols – chemical structure; fatty acids in their

composition – structure and properties.3. Phosphoglycerides – classes, structure, properties and functions.4. Sphingolipids and glycosphingolipids – classes, chemical structure,

properties and biological role.5. Dietary lipids: daily requirements, digestion and absorption. Bile's

role. Bile acids – structure role and metabolism.6. Resynthesis of lipids in intestine and blood transport. Lipoprotein

metabolism.7. Disorders of lipid digestion and absorption – causes and

consequences.8. Biosynthesis and oxidation of TAG in adipocytes – pathways,

regulation and functions.9. Fatty acid oxidation (-oxidation) of fatty acids with an even

number of carbon atoms. Reactions, regulation and role.10. Energetic yield of fatty acids -oxidation. Connection of -

oxidation with Krebs cycle and electron transport chain.11. -Oxidation of fatty acids with an odd number of carbon atoms.

Propionyl CoA oxidation.12. Oxidation of unsaturated fatty acids13. Alternative pathways for fatty acid oxidation – oxidation in

peroxisomes.14. Stoichiometry of palmitate oxidation to acetyl CoA and to CO2 and

H2O15. Oxidation of arachidonic acid16. Biosynthesis of fatty acids – characteristic of polyenzymatic

complex17. Biosynthesis of saturated fatty acid – source of acetyl CoA and

NADPH, activation of acetyl CoA and Lynen cycle18. Elongation and desaturation of fatty acids19. Biosynthesis of saturated fatty acids with an odd number of carbon

atoms20. Biosynthesis of fatty acids – partial reactions and regulation. Rate

dependence on nutrition rhythm and composition21. Acetyl-CoA shuttle system (citrate shuttle) and NADPH formation.

Regulation and importance.22. Butyric acid biosynthesis23. Arachidonic acid biosynthesis24. De novo biosynthesis of phosphoglycerides – reactions, regulation

and lipotropic factors.25. Salvage pathway synthesis of phosphoglycerides – reactions,

regulation and lipotropic factors.26. Sphingomyelin metabolism. Disorders of sphingomyelin

metabolism (Niemann-Pick disease)27. Glycosphingolipids metabolism. Disorders of sphingomyelin

metabolism (Gaucherie’s disease, Fabry's disease, ’ disease etc)28. Cholesterol. Structure. Biosynthesis, utilization and elimination

from organism29. Cholesterol and cholesterol ester – structure, mechanism and

enzyme of esterification, role and regulation30. Connections between cholesterol’s and plasma lipoprotein

metabolisms. Disorders of cholesterol metabolism – hypercholesterolemia, cholelithiases (Gallstones formation) and atherosclerosis

31. Acetyl-CoA – formation and utilization.32. Ketone bodies – nature, biosynthesis and oxidation33. Ketone bodies – oxidation, energy yield from oxidation34. Ketone bodies – structure, biosynthesis, regulation and disorders

(ketoacidosis)35. Fat-soluble vitamins, D, E and K – structure, functions and

disorders caused by their deficiency.36. Connections of carbohydrate and lipids metabolism. Schematic

show the pathway of lipid formation from glucose. Pentose phosphate shuttle's role in lipid biosynthesis.

37. Hormonal regulation of lipid metabolism – influence of insulin, glucagon and adrenaline (epinephrine)

38. Biological membranes – functions, composition, structure and properties of membrane lipids.

39. Biological membranes: carbohydrates and proteins in membranes – location, properties and functions. Fluid – mosaic theory of membrane structure.

40. Membrane properties – movement, fluidity, selective permeability, transport trough membrane.

Metabolism of simple and conjugated proteins.

1. The amino acid pool. Inputs and outputs to the amino acid pool. Nitrogen balance. Nutritional requirements in protein. Biological value of dietary proteins. Essential amino acids.

2. Protein digestion. Endo- and exopeptidases, specificity. Regulation of enzyme secretion.

3. Protein digestion – HCL role, mechanism of secretion and its regulation. Gastric's juice acidity assay. Hypochlorhydria and hyperchlorhydria

4. Absorption of amino acids from small intestine – Na-simport mechanism and -glutamate cycle.

5. Putrefaction of amino acids in intestine formation of indol, scatol, cresol and indicane. Their inactivation in liver. Mechanisms of conjugation.

6. Outputs from the amino acid pool.7. Decarboxylation of amino acids. Enzymes. Final products –

their biological activity and inactivation (serotonine, histamine, dopamine and -aminobutyric acid)

8. The disposal of amino acid nitrogen – oxidative deamination. Enzymes and coenzymes. Oxidative deamination of glutamic acid, glutamate dehydrogenase, characteristic of the reaction, enzyme and their biologic role.

9. Transamination of amino acids – role, enzyme, coenzymes and mechanism of the reaction. Medical utility of aminotransferase's activity assay.

10. Alanine and aspartate transamination – reactions, enzymes, Co-enzymes, importance. Medical utility of AST and ALT activity assay.

11. Transdeamination of amino acids. Stages, mechanism, enzymes and significance.

12. Indirect deamination of alanine13. Ammonia formation and removal. The urea cycle –

reactions, regulation and importance.14. In urea cycle – overall stoichiometry, energetic expenses

and interrelations with tricarboxylic acid cycle.15. The urea cycle – reactions, compartmentalization of the

enzymes and its significance.16. The urea cycle – reactions and significance. Daily urea

excretion of urea. Hyperammonemia – causes and consequences.

17. Glutamine and asparagine – structure and involvement in ammonia transport (reactions, enzymes and energetic expenses).

18. Ammonia removal by ammonium salt's formation. Mechanism. Interrelations with acid-base equilibrium.

19. The fate of the amino acid's carbon skeletons. Glycogenic and ketogenic amino acids.

20. The fate of the amino acid's carbon skeletons (C3 and C4)21. Essential and nonessential amino acids. Biosynthesis of

nonessential amino acids: nitrogen sources, mechanism and enzymes. Glutamine synthetase.

22. Folic acid and vit. B13 – chemical nature and role in amino acid's metabolism.

23. Metabolism of glycine, serine, treonine and alanine.24. Metabolism of cysteine and methionine.25. Metabolism of phenylalanine, tyrosine and tryptophan.

Hereditary disorders of their metabolism.26. Metabolism of decarboxylic amino acids. Their role in the

integration of metabolism.27. Amino acids as precursors of biologically important

compounds – catecholamines, melanin and creatine.28. Diseases associated with abnormal amino acid metabolism -

Hartnup's diseases, phenylketonuria, tyrosinemia, alkaptonuria, maple syrup urine disease etc.

29. Digestion and absorption of nucleo proteins. Enzymes. Final products and their fate.

30. Catabolism of purine nucleotides – reactions, enzymes, final product and its fate. Uric acid daily excretion.

31. De novo synthesis of purine nucleotides – reactions, enzymes and regulation

32. Purine salvages pathway – reactions, enzymes, significance.

33. Diseases associated with defects of purine metabolism – gout (causes, consequences and principle of treatment)

34. Catabolism of pyrimidine nucleotides.35. Biosynthesis of pyrimidine nucleotides: substrates, reactions,

enzymes, regulation and intracellular location of the reactions.36. Deoxyribonucleotide formation – reaction, role of the redoxin and

NADPH. Synthesis of deoxythymidine nucleotide.37. Hemoproteins structure (on the example of hemoglobin).

Hemoglobin's evolutive types and their role.38. Digestion and absorption of hemoproteins. Iron metabolism – role

of transferrin and ferritin.39. Hemoglobin biosynthesis – reactions up to porphobilinogen (further

without formulas) and regulation. Abnormal porphyrin biosynthesis (overview).

40. Catabolism of hemoglobin – bilirubin formation and excretion. Disorders of hemoglobin's catabolism – icteric syndrome (types, causes, disorders of bilirubin excretion and laboratory diagnosis)

Hormones. Functional biochemistry of blood

1. The hierarchy of the regulatory systems. Hormone’s place in the hierarchy of regulation of metabolism and physiological functions. Hormone's classifications. Central regulation of the hormone functions – role of hypothalamus and adenohypophysis

2. Mechanisms of action of hormones.3. Hormones – definition, overview chemical nature. Mechanism of

action of protein -peptide hormones4. Hormones – definition, overview, chemical nature. Mechanism of

action of steroid hormones.5. The hormone – receptor interaction. The receptor – adenylate

cyclase complex. Cyclic AMP function. Cyclic AMP-dependent protein kinaze and phosphorylation of cellular proteins role in the transfer of the information. cAMP phosphodiesterase activity.

6. Diacylglycerol and inositol-1,4,5 triphosphate – second messengers in the action of the hormones. Role of protein kinasic and Ca2+ in their function. Calmodulin – structure and role.

7. Adenohypophisis hormones – chemical nature, mechanism of action, regulation of secretion, biological effects.

8. Neurohypophisis hormones – chemical nature, mechanism of action, regulation of secretion, biological effects. Disorders of neurohypophisis functions.

9. Thyroid hormones: T3 and T4 – biosynthesis and release: their regulation; mechanism of action; metabolic effects; disorders of thyroid function.

10. Parathyroid hormone and calcitonine: chemical nature, regulation of secretion, mechanism of action, metabolic effects, correlation’s with other compounds that regulate calcium and phosphate metabolism. Disorders of parathyroid functions.

11. Regulation of calcium and phosphate metabolism. Vit. D: structure, metabolism, and function. Role of 1,25-dihydroxycholecalciferol. Causes and consequences of hypocalciemia and hypercalcemia.

12. Pancreatic hormones: insulin – chemical nature; biosynthesis, secretion an d their regulation; mechanism of action; metabolic effects.

13. Pancreatic hormones: glucagone – chemical nature; biosynthesis, secretion an d their regulation; mechanism of action; metabolic effects

14. Disorders of pancreas functions – diabetes mellitus – causes, types, and metabolic changes.

15. Adrenal medulla's hormones: norepinephrine and epinephrine – structure, biosynthesis, functions and cellular responses.

16. Hormones control of water – mineral metabolism: vasopressin and aldosterone – structure, regulation of secretion, metabolic effects; diabetes insipid and renal hypertension

17. Glucocorticoid hormones: structure, biosynthesis, release and their regulation, mechanism of action, metabolic effects and dysfunction.

18. Female sexual hormones – structure regulation and rhythm of secretion, mechanism of action and effects.

19. Male sexual hormones – structure mechanism of action and biological effects. Steroid anabolic

20. Prostaglandin and related compounds – nomenclature, structure, biosynthesis and functions.

21. Blood – functions and chemical composition (overview)22. Erythrocytes (red cells) - functions, peculiarities of chemical

composition and metabolism23. Leycocytes and platelets - functions, peculiarities of chemical

composition and metabolism24. Functions chemical composition and physico-chemical properties

of plasma

25. The major proteins of plasma brief characteristic, methods of separation and assay.

26. Plasma proteins – diagnostic value. Hypo-, hyper-, dis- and para-proteinemias – notion, causes and examples.

27. Blood enzymes – classification, examples and practical utility in diagnostic

28. Enzymes of diagnostic interest – organ specific enzymes in liver diseases

29. Enzymes of diagnostic interest – organ specific enzymes in heart diseases

30. Indicator blood enzymes. Mechanism of serum level increasing

31. Plasma non-proteic nitrogen compounds. Examples. Role. Ammonia and urea – content and sources. Hyperammonemia and hyperuremia – causes and consequences.

32. Mineral compounds of plasma: macro-, oligo-, and microelements – examples and role.

33. Oxygen and carbon dioxide transport – biochemical mechanisms of respiration function of blood.

34. Functional requirements to hemoglobin and cooperative binding of oxygen. Role of 2,3-diphophoglycerate

35. Disorders of oxygen transport – hypoxia – types, causes and consequences.

36. Acid-base equilibrium – buffer systems and physiological mechanisms of buffering

37. Disorders of acid-base equilibrium – acidosis and alkaloses – causes, diagnostic and mechanisms of buffering.

38. Biochemical mechanisms of blood clotting – plasmatic and platelets coagulagulation factors (brief characteristic). Intrinsic mechanism of clotting – causes timing and cascade.

39. Biochemical mechanisms of blood clotting – plasmatic and platelets coagulagulation factors (brief characteristic). Extrinsec mechanism of clotting – causes timing and cascade.

40. Fibrinolitic and anticoagulant mechanism. Vit. K role in blood clotting. Medical utility of antivitamines K