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Questions to prepare for the exam

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  1. A. Answer the following questions according to the text
  2. Answer the following questions.
  3. Answer the questions
  4. Answer the questions about passages III and IV.
  5. Answer the questions of the quiz.
  6. Answer the questions.
  7. Answer these questions.
  8. Asking Questions
  9. B). Make up 5 questions to the text in a written form.
  10. Complete the dialogue by asking questions

1. The object and problems of the biological and clinical chemistry. The concept of biochemical reactions.

2. Amino acids as the structural protein monomers. General characteristics, classification (polar, nonpolar, uncharged polar), properties.

3. The specificity of the primary protein structure. Features of the peptide bond formation. The determining role of primary structure in the formation of higher levels of organization of the protein molecule.

4. The secondary structure of proteins. Bonds that stabilize the secondary structure, α-helix. Factors violating helix formation. β-pleated sheet, special characteristics of conformational structure.

5. The tertiary structure of proteins. Bonds that stabilize the tertiary structure (covalent, ionic, hydrophobic, hydrogen, Van-der-Waals forces: the examples).

6. The quaternary structure of proteins. The concept of the monomers and oligomers.

7. The dependence of protein properties on its conformation. The relationship of structure and function. The concept of "native protein". The concept of allosteric proteins.

8. The main functions of simple and conjugated proteins in the body: structural, catalytic, receptor, regulatory, transport, protection, contractility, and others.

9. Protein content in tissues and organs. The size of the protein molecules. Methods for define protein molecular mass (gel filtration, ultracentrifugation, disc electrophoresis).

10. The proteins solubility in water. Dependence of the solubility on the amino acid composition of proteins. Physico-chemical properties of aqueous solutions of proteins. The concept of the isoelectric point.

11. Denaturation and renaturation of proteins. Denaturing agents (physical and chemical). The use of denaturation in the clinic. Protein precipitation reactions in aqueous solutions. Protein salting out. The reversibility of the process. The use of salting out in medicine.

12. Simple proteins. The principle of their classification. Globular proteins. Functions of albumin and globulins of blood plasma. Features of the structure and function of histones and protamines.

13. Conjugated proteins, their classification. Metalloproteins and their function in the body.

14. Lipoproteins, structural features, role in the construction of cellular membranes.

15. The structure of phosphoprotein, their role in metabolism. The biological significance in fetal tissues construction.

16. Glycoproteins, the structure of the prosthetic group, the biological role. Collagen.

17. The main representatives of chromoproteins. Hemoproteins: catalase, peroxidase, cytochrome oxydase, their functions in the body.

18. Hemoglobin A, structure and function. Allosteric forms of hemoglobin. Hemoglobinopathies. Structure, the functional similarities and differences between the molecules of hemoglobin and myoglobin.

19. Biochemistry of purine and pyrimidine nucleotides. Cyclic nucleotides. Distribution in the cell and biological function.

20. The nucleic acids DNA and RNA, the primary and secondary structure. Species specificity of nucleic acids.

21. Conjugated proteins. Nucleoproteins, structure and functions.

22. The chemical nature, structure and function of enzymes, cofactors and characteristics of coenzymes, and their role in catalysis.

23. The concept of the active site of enzymes. Allosteric site. Allosteric enzymes.

24. Isozymes. Multimolecular enzyme systems.

25. Units of enzyme activity. Definition of enzyme activity.

26. The mechanism of enzyme action. The theory of Fisher.

27. The mechanism of enzyme action. Koshlend theory. Substrate-strain theory.

28. Classification of enzymes. Oxidoreductases, transferases. Examples.

29. Classification of enzymes. Hydrolases, lyases. Examples.

30. Classification of enzymes. Isomerases, ligases. Examples.

31. The kinetics of enzymatic reactions. The affinity between the substrate and enzyme. Michaelis-Menten equation. The concept of the Michaelis constant.

32. Briggs - Haldane and Lineweaver-Burke equations. Restrictions on the use of the Michaelis - Menten equation.

33. Regulation of enzyme activity. Activators of enzymes.

34. The control of the enzyme amount.

35. Enzyme transformation in active forms. Chemical modification.

36. Allosteric regulation.

37. Types of enzyme inhibition: competitive reversible inhibition.

38. Non-competitive reversible inhibition. Un-competitive inhibition.

39. Irreversible inhibition of enzymes. Types of irreversible inhibition. Denaturation. Non-competitive irreversible inhibition.

40. Application of irreversible competitive inhibition of enzymes in medicine.

41. Effect of pH and temperature on the rate of enzymatic reactions. The specificity of the enzyme.

42. Importance of enzymes in the regulation of metabolism. Enzimopathy.

43. The use of enzymes in medicine.

44. Modern classification of vitamins. The biological role of vitamins. Avitaminosis, hypovitaminosis, hypervitaminosis in the human body.

45. The causes of hypo-and avitaminosis. Examples.

46. Biochemistry of vitamin A.

47. The vitamins D group, structure, properties and functions.

48. The chemical nature of vitamin E, deficiency, biological role.

49. The chemical nature of vitamin K, deficiency, functions.

50. Vitamin C, its structure, deficiency, functions.

51. Vitamin B1 chemical structure, deficiency, functions.

52. Vitamins B2, PP, chemical structure, deficiency, functions.

53. Vitamin B6, chemical structure, deficiency, functions.

54. Vitamins B12 and Bc, chemical structure, deficiency, functions.

55. Vitamin B5 (pantothenic acid), the structure, role in the body.

56. Vitamin H (biotin), the structure, properties and functions.

57. Vitamin-like substances. Examples.

58. Antivitamins, their mechanism of action, use in medicine.

59. Modern ideas about hormones, the definition, features, the classification on the chemical structure.

60. Biological membranes as supramolecular complexes. Chemical composition, structure, properties and functions.

61. Transport of substances across cell membranes: passive diffusion, facilitated diffusion.

62. Active transport of substances across the cell membrane.

63. Hormonal signal transmission: adenylate cyclase messenger system.

64. Hormonal signal transmission: phosphatidyl inositol / calcium system.

65. The mechanism of lipophilic hormones action.

66. Metabolism, anabolism, catabolism. The three phases of catabolism (digestive, the specific and common pathway of catabolism), their functions, the energy yield. The concept of key metabolites of the human body (acetyl-CoA, pyruvate).

67. General scheme of oxidative decarboxylation of pyruvic acid, the localization of the process. The structure of pyruvate dehydrogenase complex. Regulation of the process.

68. The essence of the process of biological oxidation. The localization of biological oxidation in a cell. The role of oxygen in substrate dehydrogenation (oxidation).

69. Energy-rich compounds, their classification, chemical structure, formation and functions. The universal energy source of the body - ATP, its structure, function, biological role.

70. Oxidative and substrate level phosphorylation. Modern ideas about the mechanism of oxidative phosphorylation.

71. Modern ideas about the mechanism of tissue respiration. The structure of the respiratory chain: 4 complexes and their characteristics.

72. Places of energy release in biological oxidation. Causes of a cascade of energy releasing in respiratory chain.

73. Regulation of biological oxidation.

74. Microsomal oxidation.

75. The enzymes catalase, peroxidase, superoxide dismutase, their role in the body. Oxygen toxicity, its reactive species, the mechanisms of protection.

76. The pathology of biological oxidation and bioenergetic processes. The effect of uncoupling agents, inhibitors and activators.

77. The structure of the substrates, the sequence of reactions, enzymes and reactions of the citric acid cycle (Krebs cycle).

78. The role of dehydrogenation reactions in the Krebs cycle. Relationship of the Krebs cycle and biological oxidation processes which release energy. Energy yield of the reactions of the Krebs cycle.

79. General characteristics, functions and classification of carbohydrates, the splitting of polysaccharides and disaccharides in the gastrointestinal tract.

80. Monosaccharides: structure, properties, and the projection formulas. Biologically important derivatives of monosaccharides.

81. Reserve polysaccharides. Structural polysaccharides. Glycosaminoglycans.

82. Glycogenic function of the liver, the biosynthesis and mobilization of glycogen, regulation.

83. Violations of glycogen metabolism.

84. Glycolysis. The aerobic breakdown of carbohydrates. Energetic of processes.

85. Anaerobic glycolysis. Examples, energetic of processes.

86. Shuttle mechanisms of hydrogen transport from the cytoplasm to the mitochondrion. Malate-aspartate shuttle system and glycerol phosphate shuttle system.

87. Pathways of lactate metabolism in the liver and muscles.

88. Pentose phosphate pathway.

89. Lactose and galactose metabolism. Fructose and galactose involvement in the glycolysis.

90. Differences and similarities of alcoholic fermentation and glycolysis.

91. Metabolic pathway of ethanol in the human body.

92. Gluconeogenesis, the sources, the mechanism and regulation of the process.

93. The structure of the basic lipids of human tissues: fatty acids, TAG, phospholipids, bile acids, cholesterol, etc.

94. Digestion and absorption of fats. Resynthesis of fats in the intestinal wall.

95. Formation of transport lipoproteins in the intestine. Apoproteins functions. Role of chylomicrons and VLDL in the transport of fat from the intestine.

96. Lipid metabolism. Lipogenesis and lipolysis in adipose tissue, and their regulation. The role of lipoproteinlipase and TAG-lipases. The biosynthesis of triglycerides.

97. The oxidation of fatty acids. Importance, the sequence of the reactions. Energetic of the processes. Connection with the ETC and the TCA cycle.

98. Ketone bodies. The chemical nature, role, synthesis. Causes of ketosis and ketoacidosis in diabetes and starvation. Diagnostic importance of ketone bodies determination in urine.

99. The biosynthesis of fatty acids: a sequence of reactions, the localization of process, the characteristic of enzymes, regulation.

100. Cholesterol: biological functions, synthesis, regulation.

101. The biosynthesis of bile acids as the main way of cholesterol conversion in the body. Primary and secondary bile acids. Enterohepatic circulation.

102. Lipoproteins and their role in the transport of cholesterol: endogenous and exogenous. The causes of atherosclerosis.

103. Regulation of lipid metabolism, the role of the central nervous system, hormones and vitamins.

104. Pathologies of lipid metabolism: Obesity, fatty degeneration. Hereditary diseases of lipid metabolism (dyslipoproteinemia, sphingolipidosis, etc.).

105. Protein diet. Sources and ways to use the amino acids in the body. Nitrogen equilibrium. The breakdown of tissue proteins. Reserve proteins.

106. The main stages of protein digestion in the gastrointestinal tract. The value of the secretion of proteases as proenzymes. The mechanism of the activation.

107. Common pathways of amino acids metabolism. Deamination, transamination. Using the evaluation of transaminase activity in clinical practice.

108. Decarboxylation of amino acids. Biogenic amines and their neutralization.

109. Sources of the formation and mechanisms of neutralizing ammonia in the body.

110. Ornithine cycle of urea synthesis, its role and relationship to other metabolic pathways.

111. Pathology of nitrogen metabolism (protein deficiency, hyperaminoaciduria, cystinosis, cystinuria, homogentisuria, Hartnup desease, ammoniemia).

112. Metabolism of nitrogen-free amino acids residues: oxidative cleavage of amino acids, gluconeogenesis from amino acids. Glycogenic and ketogenic amino acids. Examples. The biosynthesis of amino acids.

113. Pathways of biochemical interconversion of hydrocarbon chains of carbohydrates, proteins and fats.

114. The breakdown of chromoproteins. Hemoglobin synthesis.

115. The cleavage and absorption of nucleic acids. Catabolism of pyrimidine bases. Orotaciduria.

116. Catabolism of purine nucleotides. Gout: causes, treatment.

117. The synthesis of purine nucleotides. Regulatory reactions.

118. Synthesis of pyrimidine bases.

119. Synthesis of nucleoside-and deoxynucleoside triphosphates.

120. The DNA biosynthesis. Enzymes, protein factors. The main stages.

121. RNA biosynthesis. Processing.

122. Synthesis of DNA and RNA on the RNA template. Non-matrix synthesis.

123. Protein synthesis. The main stages.

124. Transfer of proteins across membranes. Posttranslational modification of proteins.

125. Regulation of protein synthesis.

126. Medications as inhibitors of proteins and nucleic acids synthesis.

127. Genetic engineering. Creating and using recombinant DNA.

128. Modern ideas about hormones, definition, classification (in chemical structure and mechanism of action).

129. Hormones of pituitary, their functions in the body.

130. Hormones of adrenal gland, their functions in the body.

131. Hormones of the thyroid and parathyroid glands, their functions in the body.

132. Testicular hormones, their functions in the body.

133. Ovaries hormones, their functions in the body.

134. Hormones of the placenta, their functions in the body.

135. Hormones of the pancreas and gastrointestinal hormones in the body, their functions.

136. Levels of homeostasis regulation.

137. The relationship of metabolic processes in the body.

138. Regulation of the carbohydrates, fats and amino acids metabolism with the participation of insulin, glucagon, adrenaline and cortisol.

139. Diseases associated with the violation of the hormonal regulation of fats, carbohydrates and amino acids metabolism. Main manifestations of diabetes. Biochemical changes in the body.

140. Changes in metabolism during fasting.

141. General characteristics of the calcium-phosphorus metabolism. Hormones that regulate the calcium and phosphorus metabolism: parathyroid hormone, calcitonin, calcitriol; their structure, regulation. Disorders: hypo-and hyperparathyroidism.

142. Mineral and water and salt metabolism. Functions of water in the body. The main parameters of the liquid medium of the body.

143. The chemical composition and physico-chemical properties of urine in health and disease. The diagnostic value of urinalysis.

144. The role of kidneys in maintaining constant pH and regulation of water and salt metabolism of the body. Vasopressin. The renin - angiotensin – aldosterone system. Biochemical mechanisms of renal hypertension.

145. The chemical composition of nervous tissue. Characteristic of its metabolism.

146. Chemical basis of nerve impulses conduction. Cholinergic and adrenergic synapses. Neurotransmitters, their structure, role, synthesis and transformation.

147. Structural and functional organization of the sarcomere of muscle fiber. The chemical composition of muscle tissue. Biochemical changes in muscle pathology.

148. The mechanism and energetic of muscle contraction.

149. Biochemistry of connective tissue. Its structure, functions. Biosynthesis of collagen and elastin.

150. Proteoglycans as the basis of the extracellular matrix of connective tissue. Glycosaminoglycans: structure, function. The change of the connective tissue with aging and certain pathological processes.

151. The chemical composition of bone tissue. The formation of bones. The metabolism of bone tissue.

152. The chemical composition of blood: characteristic of main protein fractions. Diagnostic importance of blood proteins. The role of albumins and globulins in the transport of substances.

153. Non-protein substances of blood: nitrogen and nitrogen-free. Total and residual nitrogen, azotemia, its types and causes. Electrolytes of blood plasma. Blood cells.

154. Buffer systems of blood and acid-base balance.

155. Respiratory function of blood.

156. Modern concepts of blood coagulation. Anticoagulation blood system.

157. Blood enzymes as biochemical indicators of visceral organs damage (myocardial infarction, muscle deseases, bone tumors, pancreatitis).

158. The chemical composition and main functions of the liver. 159. The role of the liver in the metabolism of proteins.

160. The role of the liver in lipid metabolism.

161. The role of liver in carbohydrate metabolism.

162. The chemical composition of bile and gallstones. Bile functions.

163. The metabolism of bile pigments. Jaundice categories, causes of jaundice.

164. Detoxifying liver function. Monooxygenase enzyme system. Conjugation with glucuronic and sulfuric acids.


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