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Clinical Biochemistry Exam Questions

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0% found this document useful (0 votes)
106 views7 pages

Clinical Biochemistry Exam Questions

Uploaded by

Omkar
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

Examination questions on biochemistry

for medical faculty 2nd year students

1. Subject and tasks of biological chemistry. Objects of the biochemical research. The branches of
biochemistry: bioorganic chemistry, static, dynamic and functional biochemistry, molecular biology, medical
biochemistry.
2. The primary structure of proteins: the specificity, the properties of the peptide bond. Secondary and
tertiary structure of proteins and bonds which stabilize them.
3. Quaternary structure of proteins. Examples of proteins that have the quaternary structure. The
conceptions of a protomer, oligomer. The significance of conformational changes (an assemble, dissociation
and interactions of protomers) for functions of proteins (on the example of hemoglobin, protein kinase)
Biological functions of proteins. The specific complementary “protein-ligand” interaction as a basis of the
realization of biological functions. Enzyme- substrate, hormone-receptor interactions.
4. A size and a shape of protein molecules. Globular proteins and fibrous proteins. Physical and
chemical properties of proteins: ionization, hydration, solubility, precipitations. The separation of an
individual protein: salting out, electrophoresis. Tests of the colloidal stability: thymol test, Veltman’s test.
The paper electrophoresis of blood proteins. Proteinogram.
5. Classification of proteins. Simple proteins: albumins and globulins, protamine’s, histones,
prolamins and glutelins.
6. The primary structure of nucleic acids. The junction between mononucleotides (3’,5’
phosphodiester bond). The secondary structure of DNA: bases pairing (Chargaff’s rule). Parameters of DNA
double helix. The primary and secondary structure of RNA. The biological functions of messenger, transport
and ribosomal RNA.
7. Nucleoproteins. The spatial packing of DNA molecule in a nucleoprotein (nucleosomes, solenoids).
The structure of RNA-proteins particles of ribosome.
8. Carbohydrate-protein complexes. Glycoproteins: the structure of carbohydrate component. The
linkage between carbohydrate and protein (0-, N-glycosidic bonds). Representatives of glycoprotein: the
structure and biological functions of mucus, blood glycoproteins, uroglycoproteins. The clinical importance
of determination of neuraminic acid and glycoproteins in the blood.
9. Glycosaminoproteoglycans. The structure of glycosaminoproteoglycan complexes of the
connective tissue. Glycosaminoglycans: the classification, the structure and biological functions of some
representatives.
10. Hemoproteins. The structure and function of hemoglobin. Derivatives of hemoglobin -
oxyhemoglobin, carbon monooxyhemoglobin (HbCO), carbaminogemoglobin , methemoglobin (MetHb).
Minor hemoglobins - P, F and S, hemoglobinopathies.
11. Phosphoproteins. The structure and role of the separate representatives: phosphoproteins of milk
and eggs. Protein kinases. The role of protein kinases in the regulation of the activity of the cellular proteins.
12. Structure and functions of cell membranes. Lipid composition and the structure of a lipid bilayer.
Proteins of membranes, General properties of membranes: liquid-crystal structure, asymmetry, selective
permeability. Mechanisms of carry of substances through membranes: simple diffusion, active transport
(symport and antiport), facilitated diffusion. The transmembrane transduction of hormone signals (the
mechanism of the steroid hormone action).
13. The characteristic of plasma lipoproteins: the principle structure, composition and functions.
Methods of the separation of plasma lipoproteins. The clinical importance of determination of LDL, VLDL,
CM and HDL.
14. Enzymology. Similarities and differences of enzymes and inorganic catalysts. The classification
and nomenclature of enzymes. Classification: subclasses, subsubclasses. Examples.
15. The chemical nature and the structure of enzymes. Active and allosteric (regulatory) sites.
Enzymes simple- and enzymes conjugated proteins. The chemical nature and structure of coenzyms: NADP,
FAD, FMN, CoASH, TDP, pyridoxal phosphate and THFA.
16. The Mechanism of the enzyme action. Energy changes - the effect on the activation energy. The
mechanism of enzymes action on the example of choline esterase. Enzymes specificity . Types of specificity.
The theories of specificity.
17. Kinetics of enzyme-catalyzed reactions. The Michaelis constant. Velocity of enzyme-catalyzed
reactions. The Micaelis-Menten equation. The influence of the substrate, enzyme concentration, temperature
and pH on the rate of the enzyme-catalyzed reactions.
18. The activation of the enzyme activity. Types of activation. Units of enzyme activity. Specific and
molecular activity.
19. The inhibition of the enzyme activity. Specific and non-specific, reversible and irreversible,
competitive and noncompetitive inhibitors. The Lineweaver-Burke plot.
20. Isozymes and their characteristic. Isozymes of lactate dehydrogenase (LDH). Isozymes of LDH,
creatine kinase, alkaline phosphatase in clinical diagnosis. The medical enzymology: enzymopathology,
enzymotherapy? Enzymes in clinical diagnosis. The concept of a multienzyme complex.
21. Biochemistry of nutrition. The concept of balanced diet. Essential and nonessential nutrients.
Mineral components of food: macro-, micro-, and ultra microelements. A biological role of mineral
components. The importance of the supplying of a growing organism by essential nutrients.
22. Macronutrients. The biological value of dietary proteins. The requirement, the quality of dietary
protein. Essential amino acids. The nitrogen balance. Protein malnutrition. Kwashiorkor.
23. Carbohydrates and fats as components of food, daily requirement, importance. Unsaturated fatty
acids (w-з, w-б families). A biological role of unsaturated fatty acids.
24. Vitamins. Definition. The nomenclature and classification. Functions of vitamins. Primary and
secondary hypo- and avitaminosis. Antivitamins. The mechanism of action of antivitamins.
25. Vitamin РР, structure and biological role. Daily requirement. Symptoms of avitaminosis.
Structure and mechanism of action of NAD and NADP coenzymes. NAD- dependent dehydrogenases.
26. Vitamin B1: the structure, functions, indications of avitaminosis. Thiamine diphosphate: the
structure and functions. TDP-dependent enzymes.
27. Vitamin В2: the structure, the daily requirement, indications of avitominosis. The structure and
functions of FMN and FAD. The primary and secondary flavin-dependent dehydrogenases.
28. Vitamin Вз (pantothenic acid). The structure, the daily requirement. The structure and biological
role of coenzyme A.
29. Vitamin Н: the structure, the biological role, sings of avitaminosis. The participation of biotin in
processes of carboxylation. Carboxylation of acetyl CoA to malonyl CoA
30. Vitamin В6: pyridoxine, pyridoxal, pyridoxamine. The structure and the biological role. The
coenzyme pyridoxyl phosphate: the structure and mechanism of the action in the transamination of amino
acids.
31. Folic acid. The structure, daily requirement and biological role. Biochemical functions of THFA
in the transfer of one-carbon units..
32. Vitamin B12. The structure and daily requirement. Avitaminosis and the cause of it’s occurrence.
The intrinsic factor (transcorrin), it’s role in absorption of vitamin B12. Biochemical functions of vitamin B12.
33. Lipoic acid: the structure, property and biochemical functions. The participation in the oxidative
decarboxylation of pyruvate.
34. Vitamin C (ascorbic acid). The structure, daily requirement, food sources, avitaminosis.
Participation in redox reactions, steroidogenesis and in the maturing of collagen (hydroxylation of prolyne
and lysine residues).
35. Vitamin A. The structure, symptoms of avitaminosis and hypervitaminosis. The daily
requirement, the absorption and transport of vitamin A in the blood. Carotenes as a precursors of vitamin A.
A role vitamin A in the vision, in processes of cell proliferation.
36. Vitamins D2 and D3. Precursors of vitamin D: ergosterol and 7-dhydrocholesterol,
photochemical transformation of vitamins D2 and D3. Formation of active forms of vitamin in the liver and
kidneys. The hormone-like mechanism of action of vitamins D. The daily requirement. Signs of avitaminosis
and hypervitaminosis of vitamin D.
37. Vitamins Е.The structure, signs of avitaminosis, food sources, daily requirement. Biological
function. Synthetic antioxidant molecules.
38. The exchange in substances and energy as a whole integrated system. The classification of
organisms according to energy sources and carbon sources. Exergonic and endergonic reactions. ATP as a
universal carrier of energy.
39. High-energy bonds. Types of high-energy compounds. A structure of nucleoside triphosphates.
ATP as a universal high-energy compound. Structure of creatine phosphate. Synthesis of creatine and
creatine phosphate. A biological role of creatine phosphate.
40. Stages of the unification of energy substrates. Oxidative decarboxylation of pyruvate. The
composition of the multienzyme complex, sequence of reactions. The energy yield (in the number of ATP
molecules) .
41. The tricarboxylic acids cycle. The sequence of reactions of the Kreb’s cycle. The connection of
the TCA-cycle with processes of the oxidative phosphorylation. The concept of a subsrate-linked
phosphorylation. The energy yield of the TCA cycle and the regulation of the TCA-cycle.
42. Biological oxidation. Dehydrogenation of substrates as a first step of the biological oxidation. The
characteristic and structure of NAD and FAD-liked dehydrogenases.
43. The sequence of reactions in the respiratory chain of mitochondria. Redox-potentials and
respiratory complexes. Structure and properties of ubiquinone. Structure and properties of cytochromes and
cytochrome a3.
44. The mechanism of the oxidative phosphorylation. The coefficient of the oxidative
phosphorylation, uncoupling agents.
45. Microsomal oxidation. A sequence of reactions of the monooxygenase way. The characteristic of
components of a microsomal oxidation. Cytochrome Р 450. Properties, structure. Biological importance of
microsomal oxidation.
46. The process of the free radical oxidation. Reactive oxygen species (ROS) - superoxide radical,
hydrogen peroxide, hypo halides.
47. Lipid peroxidation, the free chain mechanism. The role of lipid peroxidation in the normal and
pathological processes. Enzymatic and nonenzymatic antioxidant system (superoxide dismutase, catalase,
peroxidase, glutathione transferase.
48. The digestion of dietary carbohydrates - enzymes, conditions. The absorption of monosaccharide
in the intestine (the mechanism). Digestive enzymes deficiencies (lactose, sucrose intolerance). The fate of
glucose within the cell.
49. Biosynthesis of glycogen. Stages and enzymes. The glycogen degradation ways. Key enzymes of
the glycogen synthesis and degradation. The regulation of glycogen metabolism. Glycogen storage diseases.
50. Anaerobic glycolysis: stages, enzymes, rate-limited reactions. The energy yield (the number of
ATP molecules).The biological significance of anaerobic glycolysis.
51. Glycogenolysis. The characteristic of separate stages. Enzymes. The energy yield.
52. Aerobic dichotomic oxidation of glucose (aerobic glycolysis): stages, their location. The energy
yield (in ATP molecules). Glycerophosphate shuttle as a carrier of hydrogen from a cytoplasm to
mitochondria
53. The fate of end products of the glucose dichotomic oxidation:(H2O,CO2, lactate). The Cory cycle.
54. The alcoholic fermentation of glucose as a way of it’s anaerobic dichotomic oxidation. Reactions,
enzymes, the energy yield. The glycerol oxidation: reactions, enzymes, the energy yield.
55. Gluconeogenesis, by-passes of glycolysis. The key enzymes, the biological role, regulation. The
resynthesis of glucose from lactate, glycerol, alanine.
56. Pentose phosphate pathway (PPP). Oxidative and non oxidative phases: reactions, enzymes. The
significance of PPP for the biosynthesis of lipids, nucleotides and microcomal oxidation.
57. The metabolism of fructose and galactose. Inherited defects of fructose and galactose metabolism.
Transitional and inherited fructosuria, galactosemia and galactosuria
58. The regulation of glucose and glycogen metabolism. The influence of adrenaline, glucagons,
glycocorticoids, insulin.
59. The dietary fat: the daily requirement, digestion and absorption. Resynthesis of triacylglycerol
within enterocytes. Chilomycrons, very low density lipoproteins. Lipoprotein lipase. The role of bile acids in
the digestion of lipids.
60. Degradation and synthesis of triacylglycerols (TAGs). The synthesis of TAGs in adipocytes. The
regulation of lipolysis and lipogenesis, key enzymes.
61. The sources and the use of glycerol.
62. Oxidation of free fatty acids - stages, reactions. The role of carnitine.
63. The sources and the use of acetyl CoA. Keton bodies. Regulation of biosynthesis. The biological
role of keton bodies. Ketonemia and ketonuria.
64. Biosynthesis of fatty acids: sequence, fatty acids activation, physiological significance.
Polyunsaturated fatty acids (vitamin F). Signs of deficiency.
65. Metabolism and functions of cholesterol. Biosynthesis of cholesterol: reactions’ sequence
including mevalonic acid formation, scheme of the further stages, key enzyme, regulation of biosynthesis. A
role of blood lipoproteins in transport and metabolism of cholesterol.
66. Cholesterol esterification in both plasma and cells by the aid of enzymes LCАТ and АCАТ,
respectively. Features of cholesterol metabolism in skin, sexual glands, adrenal cortex and liver. Synthesis of
bile acids. Structure of both primary and secondary bile acids. Conjugated bile acids. Removal of bile acids
and cholesterol from an organism . A biological role and enterohepatic circulation of bile acids .
67. Metabolism of complex lipids. Digestion, absorption, tissue decomposition and synthesis of
phosphatidyl glycerols. Ways of phospholipids synthesis. Role of both CTP and phosphatidic acid in
biosynthesis. Coupling of phosphatidylglycerol biosynthesis with synthesis of triacyglycerols in liver.
Lipotropic factors.
68. Digestion of proteins in gastrointestinal tract. Proteolytic enzymes: pepsin, gastrixin, trypsin,
chymotrypsin and peptidases. Mechanisms of their activation. pH optimum for their action, substrate
specificity. Amino acids absorption in intestine.
69. Diagnostic importance of biochemical analysis of both gastric and intestine juices. Pathological
components of gastric juice, diagnostic significance of their qualification.
70. Protein purification in large intestine. Formation, absorption in blood and neutralization in liver of
putrification toxic products: phenol, skatoxil, indoxil, cadaverin, etc.
71. Concept of amino acid cellular metabolic pool. Transamination of amino acids. Structure of
coenzyme, the transamination mechanism (with participation of pyridoxal phosphate). Specificity of
transaminases. Biological importance of transamination . Diagnostic importance of quantification in blood
serum both АlAТ and АsAТ activity.
72. Deamination ways in the living systems. Direct and indirect oxidative deamination of amino
acids. Sequence of reactions, enzymes, a biological importance.
73. Formation ways and neutralization of ammonia. Synthesis and decomposition of glutamine.
Neutralization of ammonia in liver. Urea biosynthesis. Interconnection of urea cycle and TCA cycle.
74. Specific metabolic conversions of glycine, methionine, their role in one-carbon groups formation.
Participation of tetrahydrofolic acid in these processes. Folic acid deficiency. Mechanism of bacteriostatic
actions of sulfonamides medicines. S-adenosyl methionine (SAM) as a donor of methyl groups in synthetic
reaction.
75. Metabolism of both phenylalanine and tyrosine. Formation of phenylpyruvate, phenyllactate,
phenylacetate and benzoic acids. Role of tyrosine on synthesis of catecholamine’s, thyroxin, melanin’s.
Tyrosine decomposition up to fumaric and acetoacetic acids. Hereditary disorders of phenylalanine and
tyrosine metabolism.
76. Decarboxylation of amino acids. Formation of biogenic amines: histamine, tryptamine, serotonin,
GABA. Role of biogenic amines in regulation of metabolism and physiological function, participation in
synaptic transmission of nervous impulses. Inactivation of nervous biogenic amines.
77. Biosynthesis of purine nucleotides: an origin of purine rings atoms, an initial stages of
biosynthesis (from rybose-5-phosphate up to 5-phosphorybosilamine). Salvage ways of purine nucleotides
synthesis. Regulation of biosynthesis. Purine nucleotides decomposition. Hyperuricemia and gout.
78. Biosynthesis and decomposition of pyrimidine nucleotides. Salvage ways of pyrimidine
nucleotides synthesis. Regulation of pyrimidine nucleotides biosynthesis. Orotate and methyluracil as non-
specific anabolics.
79. Replication of DNA, conditions, its mechanism and biological significance. DNA-polymerases.
Replicational folk. Replication and phases of a cellular division cycle. Damage of a DNA. Reparation of
damaged sites of DNA. Features of synthesis of DNA in eukaryotes.
80. Biosynthesis of RNA (transcription): conditions, the mechanism and biological significance.
Description of the stages: initiating, elongation, termination, posttranscriptional processing of m-RNA.
81. Biosynthesis of proteins. Activation of amino acids, substrate specificity of amino acyl-tRNA-
synthetases, adapting function of tRNA. Translation, stages (initiating, elongation, termination). Energy
sources. Role of specific protein factors in translation. Posttranslational maturation protein molecules.
Concept about chaperons.
82. The concept “one gene - one protein” as the basic postulate of molecular biology. Genetic code,
its main properties. Molecular mechanisms of genetic variability: molecular mutations, types. Mutagenic
factors. Molecular mechanisms of hereditary diseases development: a cycle-cell anemia, inborn intolerance
of sucrose, glycogenosises, etc.
83. Regulation of genes activity. Concept about operon and regulation in transcriptional level. A
structure and functioning lactose operon of [Link] (Jacob and Monod scheme). Cellular differentiation and
ontogenesis as result of genes activity regulation. Role of hormones in regulation of genes activity.
84. Decomposition of cellular proteins. Half-life time of various proteins. Lysosomal proteolytic
enzymes - cathepsins. Role of lysosome damages in inflammation and other pathological processes.
85. Digestion and absorption of hemoproteins. Features of absorption and an exchange of iron.
Hemoglobin synthesis.
86. Hemoglobin decomposition and formation of bile pigments. Distinctive properties of direct and
indirect bilirubin. Jaundice, differential biochemical diagnostics of various jaundice types. Physiological
jaundice of newborns.
87. Hormones: definition, classification. Differences of protein and steroid hormones action
mechanism. The characteristic of peptide and steroid hormones receptor complexes.
88. Secondary messengers (intracellular intermediates) of hormones. Cyclic АМP, its formation and
hydrolysis. Adenylate cyclase, phosphodiesterase. cАМP action on protein kinases.
89. Calcium as secondary messenger of hormones. Calmodulin. Formation and action of both
inositoltriphosphate and diacylglycerol as intracellular messengers of hormones action.
90. Central regulation of endocrine systems. Neuroendocrine system. Liberins, statins of
hypothalamus. Hormones of hypophysis anterior lobe: somatotropin, thyrotrophic hormon. Structure and a
biological role, influence on metabolism, hypo- and hyperproduction symptoms.
91. Gonadotropic and lacticotropic hormones of hypophysis anterior lobe. Biological role, influence
on metabolism. Features of these hormones synthesis and secretion.
92. Hormones of middle and posterior lobe of hypophysis. Structure, features of biological action.
Symptoms of hypo-and hyperproduction.
93. Hormones of epiphyses: structure, biological role.
94. Hormones of thymus: structure, biological role.
95. Structure, synthesis and a metabolism of iodothyronines, their influence on metabolism. Role of
iodothyroglobulin. Regulation of T3 and T4 liberation. Hypo- and hyperthyroidism.
96. Hormonal regulation of calcium and phosphates metabolism. Parathyroid-hormone and calcitonin,
mechanism of their action, symptoms of hypo-and hyper production. Vitamin D hormone-like action.
97. Hormones of pancreas. Insulin, structure, influence on metabolism, hypo-and hyper production
symptoms. Conversion of proinsulin into insulin. Insulin action mechanism.
98. Hormones of pancreas: glucagon, somatostatin, pancreatic polypeptide. Structure, biological
action. Influence of glucagon on metabolism. Glucagon action mechanism.
99. Hormones of adrenal glands medullar part: structure, biosynthesis, influence on metabolism. Both
adrenaline and noradrenaline action mechanism.
100. Adrenal cortex hormones. Classification, structure, influence on metabolism, ways of formation
and a metabolism of glucocorticoids.
101. Adrenal cortex hormones: mineralocorticoids, adrenocorticosteroids, estrocorticosteroids.
Structure and influence on metabolism.
102. Male and female sex hormones: structure, physiological action of androgens, estrogens and
progestins, their influence on metabolism. Concept about sex hormones’ biosynthesis and metabolism.
103. Derivatives of eicosopolyenic acids. Cyclooxygenase and lipooxygenase pathways of
arachidonic acid metabolism. Prostaglandins, prostacyclin’s, thromboxanes, leukotrienes. Structure,
classification, biosynthesis, biological role.
104. Concept about tissue hormones, hormone-like substances, hormonoids. Chemical structure and
role of gastrin, secretin, erythropoietin, angiotensin, kinines, leptine. Structure, the mechanism of formation
and decomposition, biological role. Concept about cytokines.
105. Regulation of glucose blood concentration. Formation and use ways of blood glucose. Influence
of insulin, glucagon, adrenaline and cortisol on glucose blood level. Hypo- and hyperglucemia, the reasons of
their appearance. Determination of tolerance to glucose at diagnostics of a diabetes mellitus (glucose-
tolerance test). Hypercorticism and steroidal diabetes.
106. Regulation of carbohydrates, fats, proteins metabolism by insulin, glucagon, adrenaline, cortisol.
Changes of these hormones concentration depending on feeding rhythm. Changes of the both hormonal status
and a metabolism at absolute starvation.
107. Integration of carbohydrates, fats and protein metabolism. Interconnection points of glucose and
fat metabolism, carbohydrates and amino acids metabolism, amino acids and fat metabolism. Significance of
TCA cycle, PPP and gluconeogenesis for metabolism integration.
108. Diabetes mellitus. Types, ethyologic factors of their development, main symptoms. Disturbances
of carbohydrates, fat, amino acids metabolism. Mechanisms of ketonemia, ketonuria, hypercholesterinemia,
hyperglycemia development. Glycosylated proteins. Their significance at appearance of angiopathy. Sugar
curves in diagnostics of a diabetes mellitus.
109. Features of fat metabolism in adipose tissue. Regulation of metabolism in a fatty cell (insulin,
adrenaline, noradrenaline). Disturbances of metabolism at both obesity and starvation.
110. Cellular (primitive) mechanisms of metabolism regulation. Regulation by retro inhibition
principle. Pasteur's effect. Regulation by change of concentration of substrate, enzyme, coenzyme.
111. Water-salt metabolism. Content, distribution in the body, biological role of water. Classification
of mineral elements: macro-, micro-and ultra micro elements. Concept about endemic diseases: endemic
goitre, caries, fluorosis. Hormonal regulation of water-salt metabolism. Both vasopressin and aldosterone
action mechanism.
112. Respiratory function of blood: mechanism of both oxygen and carbon dioxide transport by
hemoglobin.
113. Hemostasis system. Characteristic of main structural-functional hemostasis components:
endothelium, thrombocytes, main thrombocyte factors of hemostasis, blood clotting plasma factors. Vitamin
K, structure. K-vitamin dependent factors, role of vitamin K in their posttranslational modification, γ-carboxy
glutamic acid.
114. Extrinsic and intrinsic blood clotting ways. Cascade mechanisms of clotting reactions. First,
second and third phases of a secondary hemostasis. Biochemical mechanisms of fibrin – polymer formation.
115. Anticoagulant system. Anticoagulants: calcium-binding, antivitamins K, antithrombin and
heparin. Fibrinolysis system. Concept about disseminated blood coagulation syndrome.
116. Biochemistry of liver. Role of liver in metabolism of proteins, carbohydrates, lipids.
117. The principal mechanisms of substances neutralization in an organism: the first and second
neutralization phase, microsomal oxidation, conjugation reactions. Examples of foreign molecule
neutralization (xenobiotic) and endogenic toxins.
118. Intercellular matrix proteins: collagen, elastin. Biosynthesis and maturing of collagen.
Participation of vitamin C in collagen synthesis. hydroxiproline excretion as mark of collagen decomposition
rate.
119. The structural organization and the main functions of both an intercellular matrix and connective
tissue. Proteoglycans, glycosaminoglycans.

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