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RUDN University Medical Institute Medical faculty T.T.Berezov Biochemistry department Programme Discipline: Biochemistry: molecular mechanisms of cancer Biochemistry Programme is designed for students interested in obtaining a Ph.D. in Biochemistry. direction 06.06.01 «Biological sciences», profile «Biochemistry» (03.01.04) Qualification: Researcher. Lecturer-researcher Introduction This research programme enables the studets to progress their understanding of biochemistry and molecular biology to an advanced level and to contribute to the progression of research in this specialist field. The practical laboratory skills the students develop on this programme will be vital to their study and transferable to research roles in industry. A structured programme of training enables the students to enhance theirs abilities in scientific writing, critical thinking, experimental design and quantitative research methods. Our department offers in-depth coursework and diverse research opportunities that focus on understanding the biochemical mechanisms of life’s critical molecular processes. Research in our laboratories exposes our students to a variety of the latest methods for sophisticated biochemical analysis, including mass spectrometry, microcalorimetry, microarrays, fluorescence activated cell sorting, light scattering, and spectroscopic methods, as well as modern methods for cell culture, protein purification, and reconstitution of biochemical complexes and reactions. The flexibility of our training program allows students to train in a number of exciting research areas, and often allows students to develop highly effective interdisciplinary collaborations, resulting in cutting edge thesis projects. 1. Goal of the discipline: to form the systematic knowledge about the molecular mechanisms of biological system functions, to accommodate creation of the base for the further study medical and clinical disciplines 2. Linkages with the other subjects: The program is an interdepartmental major between biology and chemistry that emphasizes the importance of a solid foundation in the natural sciences, including mathematics and physics. The major focuses, however, on disciplines within biology and chemistry, ranging from cell biology and molecular biology to analytical chemistry and physical chemistry. 3. Course Competencies: a) Universal competences (UC) the capacity for critical analysis and evaluation of modern scientific achievements, the ability to generate new ideas when solving research and practical problems, including in interdisciplinary areas (UC-1); ability to design and realize a complex research, (UC-2); the ability to plan and solve problems own professional and personal development (UC-3) b) General professional competences (GPC) The ability to independently carry out research activities in relevant professional field with the use of modern research methods (GPC-1); an ability for teaching at the basic educational programs (GPC-2). c) Professional competences (PC) The ability to understand modern problems in biochemistry and use the fundamental biological performance in the sphere of professional activities (PC-1); An independent analysis of available information, the identification of the fundamental problems, setting goals and objectives of the study; the performance of the laboratory of biochemical research at solving specific problems for specialization with the use of modern equipment and computing resources (PC-2); An availability of skills formation of teaching material, lectures, willingness to teach in higher education and the management of research projects students, the ability to provide teaching material in verbal, written and graphic form(PC-3) As a result of study a postgraduate students have: To know: physical and chemical nature of the processes occurring in living organisms at the molecular, cellular, tissue and organ levels; structure and chemical properties of the major classes of biologically important organic compounds; major metabolic pathways converting carbohydrates, lipids, amino acids, purine and pyrimidine bases, the role of cell membranes and transport systems in metabolism; Structure and function of the most important chemical compounds (nucleic acids, natural proteins, and water-soluble vitamins, hormones, etc.); physical and chemical methods of analysis in medicine (titration, chromatographic, spectrophotometric); the role of biogenic elements and their compounds in living organisms; Chemistry of hemoglobin, its participation in gas exchange and maintaining acid-base balance; the theoretical foundations of computer science in medical and biological systems, the use of information and computer systems. To be able to: use of educational, scientific, popular scientific literature, the Internet portal for academic and professional activities; use of physical, chemical and biological equipment; to make calculations based on the results of the experiment, carried out an elementary statistical analysis of experimental data; classify chemicals based on their structural formulas; to predict the direction and the result of physical and chemical processes and chemical reactions of biologically important substances; use the IUPAC nomenclature for compiling the names of the formulas typical representatives of biologically important substances; differentiate in serum levels of normal values metabolites (glucose, urea, bilirubin, uric acid, lactic acid and pyruvic et al.) of pathologically changed, read proteinogramma and explain reasons for the differences; interpret research data. To master: chemical and biochemical terminology; basic technology of a research and transformation of information, including with the use of educational resources training; the concept of restrictions on the reliability and specificity of the most common laboratory tests; skills of setting the preliminary diagnosis based on the results of biochemical studies of human biological fluids. 4. Total efforts and Employments Total efforts ___4_credits (144 hours) № Educational work Hours (total) Semester 1 1. Employments (total) 80 including: 40 - 1.1 Lectures 1.2 Other classes 2 40 - - 40 20 20 Practical works (PW) 40 20 20 - - - - including: 1.2.1 1.2.2 Seminars (S) 1.2.3 2. Laboratory works (LW) In the interactive form (IF): 20 10 10 Individual employments (total) 64 32 32 144 72 72 4 2 2 Total efforts (hours) Credits 5. Content of the discipline 5.1. Content of the items 1. Introduction. Proteins: structure, properties, functions Biomolecules. The most important problems of current biochemistry. Methods of investigations in biochemistry. Biochemistry and Medicine. Structure and Function of Biomolecules. Proteins - essential constituents of the living cells. Physical and chemical properties of proteins. Composition and properties of amino acids and peptides. Four levels of structural organization of proteins. The three-dimensional structure of proteins; role of domens and the relationship of proteins structure to their biological functions. Methods of isolation and purification ojf proteins. 2. Complex proteins, Nucleic acids, Enzymes Classification of proteins: simple and conjugated proteins, composition and properties of individual representatives of conjugated proteins. Nucleic acids. Physico-chemical properties, composition, structure and biological role of DNA andRNA. Enzymes: general properties, chemical structure, active centers, classification and nomenclature, allosteric enzymes. The mechanisms of enzymatic catalysis. Structure and function of coenzymes, Kinetics of enzymatic reactions and methods for determination of the enzymes activity, Inhibitors of enzymes, Isoen-zymes. Regulation of the enzyme activity, Diagnostic enzymoiogy; enzymes as drugs. 3. Molecular mechanisms of regulation Vitamins: distribution, biological role, classification. Social basis of vitamin deficiency in some developing countries. Principles of vitamin therapy. Antivitamins. Composition and properties of individual representatives of the fat-soluble and witer-soluble vitamins: A, D, E. K, B1, B2, В6, B12, C, P, PP, H and Folic acid, Vitamin-like substances. Methods of quantitative determination of vitamins in the body. Hormones: hormone production in the endocrine glands. Molecular endocrinology. Mechanisms of hormonal regulation of metabolism and role of the second messengers, Chemical structure and properties of die main hormones. 4. Lipids: structure, properties, functions. Biological membranes Hydrolyzable lipids. Non-hydrolyzable lipids. Biological roles. Fatty acids and fats. Structure of phospholipids and glycolipids. Isoprenoids. Sterols. Steroid hormones. Bile acids. 5. Energy metabolism Catabolism and anabolism. Methods of metabolism investigations. Types of metabolism and its regulation. Free energy of ATP hydrolysis. Biological oxidationreduction reactions, Chemistry of digestion. Social aspects of the rational nutrition problems. 6. Carbohydrate metabolism Carbohydrate metabolism: pathways of absorbed monosaccharaides. The pathway of glycogen synthesis and degradation. Anaerobic metabolism: glycolysis, glycogenolysis and gluconeogenesis. Aerobic metabolism: pentose phosphate pathway of glucose oxidation; oxidative decarboxylation. of pyruvate, the tricarboxylic acid cycle. Biological oxidation, The respiratory chain of electrons and protons transport, Oxidative phosphorylation. Energy effect of anaerobic pathways of carbohydrate metabolism. Hormonal regulation of carbohydrate metabolism. Pathology of carbohydrate metabolism, 7. Lipid metabolism Lipid metabolism: pathways of the absorbed products lipid digestion, Mechanism of b-oxidation of fatty acids, Biosynthesis of fatty acids, triacylglycerols, phospholipids and cholesterol. Energy effect of lipid oxidation, Relationship between lipid metabolism and carbohydrate metabolism. Intracellular lipids and blood serum lipids. Regulation of lipid metabolism, Pathology of lipid metabolism. 8. Protein catabolism Protein metabolism,' dynamic state of body proteins. Nitrogen balance. Problems of adequate, balanced nitrogen nutrition. Proteolysis. Absorption and active transport of ammo acids. Pathway of amino acids metabolism in the body: reactions of deamination, decarboxylation, transamination and hydroxylation. Degradation of tissue proteins. Urea cycle. Metabolism of nucleoproteins and chromoproteins. Biosynthesis and decomposition of heme. Synthesis of purine and pyrimidine nucleotides; 9. Amino acid metabolism Metabolism of individual amino acids. Regulation of protein metabolism, Pathology of protein metabolism, Relationship of protein metabolism with metabolism of lipids and carbohydrates. 10. Biochemistry of organs and tissues Blood: composition and functions. Cellular elements. Blood plasma: composition. Plasma proteins. Carrier electrophoresis. Erythrocyte metabolism. Distribution of iron. Hydrogen ion concentration in the blood Plasma. Buffer systems in the plasma. Blood clotting. Fibrinolysis. Blood groups: the ABO system. The family of connective-tissue cells. Extracellular proteins. Metabolism of the collagens. Fibronectins. Proteoglycans. Bone and teeth. Functions of calcium. Bone remodeling. Calcium homeostasis. Structure of nerve cells . Signal transmission in the CNS . Neurotransmitters and neurohormones. Resting potential and action Potential. Receptors for neurotransmitters. Energy metabolism of the brain. Organization of skeletal muscle. Mechanism of muscle contraction . Control of muscle contraction. Energy metabolism in the white and red muscle fibers. Functions of the kidneys . Urine formation . Organic components and Inorganic components of the urine. Functions in the acid–base balance: Proton excretion and Ammonia excretion. Electrolyte and water recycling. Renal hormones. Renin–angiotensin system. Biochemistry: molecular mechanisms of cancer. 5.2. Items of the discipline and types of the works № Item Introduction. Proteins: structure, properties, functions Complex proteins, Nucleic acids, Enzymes Molecular mechanisms of regulation 4 Practical and laboratory works PW/S LW IF 4 2 4 4 - 2 6 4 4 - 2 6 4 4 - 2 6 5 Lipids: structure, properties, functions Biological membranes Biological oxidation 4 4 - 2 6 6 Carbohydrate metabolism 4 4 - 2 6 7 Lipid Metabolism 4 4 - 2 6 8 Protein catabolism 4 4 - 2 6 9 Amino acids metabolism 4 4 - 2 6 10 Biochemistry of organs and tissues 4 4 - 2 10 40 - 20 64 1. 2. 3 4 Lect ures 40 Total ISW 6 Hou rs 144 5.3. Practical classes (seminars) № п/п 1 2 Item Introduction. Proteins: structure, properties, functions Complex proteins, Nucleic acids, Enzymes Hours Practical classes Color reactions used for identification of protein and amino acids. The protein precipitation reactions The quantitative determination of protein. Dialysis of protein. The paper chromatography of amino acids. Isolation of DNA from yeast cells Effect of amylase on starch. Influence of temperature on amylase activity Determination of alkaline phosphotase activity. 4 4 3 Molecular mechanisms of regulation 4 Lipids: structure, properties, functions Biological membranes Biological oxidation 5 6 Carbohydrate metabolism 7 Lipid Metabolism 8 Protein catabolism 9 Amino acids metabolism 10 Biochemistry of organs and tissues Quantitative determination of vitamin C in potatoes, and vitamin P in tea Spectrophotometric determination of NADH and calculation of purity of commercial preparation Effect of hormones on glucose concentration in blood. The quantitative determination of lecitins in blood serum (Blure Method). Quantitative determination of cholesterol in blood serum 4 Determination of succinate dehydrogenase activity in muscle. Quantitative determination of pyruvate in urine Specificity of amylase and sucrose action. Quantitative determination of glucose in blood. Construction of sugar curves. Kinetics of lipase action The quantitative determination of malonate dialdehyde in blood serum. Determination of gastric juice acidity The quantitative determination of urea in urine The quantitative determination of creatinine in urine. The quantitative determination of aspartate and alanine aminotransferase activity in the blood serum. Determination of phenylalanine in serum by chromatography. Chromatography of amino acids. Determination of bilirubin in blood serum The quantitative determination of lactate dehydrogenase and choline esterase in blood serum. Determination of uric acid in urine Normal and pathological components of urine. Determination of amilase activity in urine 4 Total (hours) 4 4 4 4 4 4 40 6. Educational and methodical literature, programs a) Literature 1. T.T. Berezov and B.F.Korovkiv. Biochemistry. – M., Mir Publishers. -1992. -515 p. 2. Baynes J. W.Medical Biochemistry. - Third Edition; - London: Elsevier, 2009. - 653 р. 3. Kuznetsova O.M., Berezov T.T., Chernov N.N. Laboratory Manual on Biochemistry. Part 1. -М.: D IGITPRESS.-2014. -58 p. 4. Kuznetsova O.M., Berezov T.T., Chernov N.N. Laboratory Manual on Biochemistry. Part 1. -М.: D IGITPRESS.-2015. -52 p. 5. Berezov T.T., Chernov N.N. Kuznetsova O.M. Collection of biochemistry tests . – M. Изд-во «Оргсервис-2000». -2011. - 60с. 6. Principles of Biochemistry 4nd ed./ Lehninger, A.L., Nelson, D.L., Cox, M.M..Worth Publishing, 2004. 7. Principles of Medical Biochemistry 2nd ed./ Gerhard Meisenberg, William H. Simmons. - Mosby Elsevier, 2006 b) Software 1. Operating system «Windows 8» 2. Software application package «Microsoft Office» 3. Testing programme «Mentor» 4. Computer programme Pharmtest; MyTestPro c) data bases, information, reference and search systems: 1. Educational portal of the PFUR: http://web-local.rudn.ru/weblocal/kaf/rj/index.php?id=86 2. U.S. National Library of Medicine National Institutes of Health: http://www.ncbi.nlm.nih.gov/pubmed/ 3. Scientific electronic library: http://elibrary.ru/defaultx.asp 4. Electronic library system of the PFUR: http://lib.rudn.ru:8080/MegaPro/Web 5. IQlib http://www.iqlib.ru 6. Scientific electronic library Elibrary http://elibrary.ru 7. Google Academy - http://scholar.google.ru/ 8. http://vak.ed.gov.ru/ 7. Equipment and Material support of the educational process The Hitachi F-2700 Fluorescence Spectrophotometer; Microplate Absorbance Reader TransBlot Turbo (Biorad); iMark (Biorad) xMark (Biorad); VIP Freezer MDF-U33V (Sanyo - Panasonic); Double Beam Spectrophotometer U-2900 Photoelectric Colorimeters, centrifuges, thermo blocks, measuring burets, drying ovens, analytical balances, Magnetic stirrers. Automatic pipettes with dispenser and others. 8. Methodological recommendations on discipline study organization Medical biochemistry is biochemistry related to human health and disease. Its applicative arm is clinical chemistry, a field that focuses on the methodology and interpretation of chemical tests performed to support diagnosis and treatment. The study of the discipline is organized according to credit-modular system using the appropriate laboratory equipment, computers, multimedia installations. 9. Evaluation resources 1. Main terms and notions 1.1 Abbreviations ACP Acyl carrier protein ACTH Adrenocorticotropic hormone (corticotropin) ADH Antidiuretic hormone (adiuretin, vasopressin) ADP Adenosine 5-diphosphate AIDS Acquired immunodeficiency syndrome ALA 5-Aminolevulinic acid AMP Adenosine 5-monophosphate ATP Adenosine 5-triphosphate BPG 2,3-Bisphosphoglycerate cAMP 3,5-Cyclic AMP cDNA Complementary DNA CDP Cytidine 5-diphosphate cGMP 3,5-Cyclic GMP CMP Cytidine 5-monophosphate CoA Coenzyme A CoQ Coenzyme Q (ubiquinone) CTP Cytidine 5-triphosphate DAG Diacylglycerol DNA Deoxyribonucleic acid ER Endoplasmic reticulum FAD Flavin adenine dinucleotide FMN Flavin mononucleotide GABA γ-Aminobutyric acid GDP Guanosine 5-diphosphate Glut Glucose transporter GMP Guanosine 5-monophosphate GSH Reduced glutathione GSSG Oxidized glutathione GTP Guanosine 5-triphosphate Hb Hemoglobin HDL High-density lipoprotein HIV Human immunodeficiency virus HMG-CoA 3-Hydroxy-3methylglutarylCoA hsp Heat-shock protein IDL Intermediate-density lipoprotein IFN Interferon Ig Immunoglobulin IL Interleukin InsP3(IP3) Inositol 1,4,5-trisphosphate Km Michaelis constant LDH Lactate dehydrogenase LDL Low-density lipoprotein MAP kinase Mitogen-activated protein kinase mRNA Messenger ribonucleic acid NAD+ Oxidized nicotinamide adenine dinucleotide NADH Reduced nicotinamide adenine dinucleotide NADP + Oxidized nicotinamide adenine dinucleotide phosphate NADPH Reduced nicotinamide adenine dinucleotide phosphate NeuAc N-acetylneuraminic acid PAPS Phosphoadenosine phosphosulfate PDH Pyruvate dehydrogenase PEP Phosphoenolpyruvate Pi Inorganic phosphate PK Protein kinase PLP Pyridoxal phosphate PRPP 5-Phosphoribosyl 1-diphosphate PTH Parathyroid hormone Q OxidizedcoenzymeQ(ubiquinone) QH2 Reduced coenzyme Q (ubiquinol) rER Rough endoplasmic reticulum RES Reticuloendothelial system RNA Ribonucleic acid ROS Reactive oxygen species rRNA Ribosomal ribonucleic acid SAH S-adenosyl L-homocysteine SAM S-adenosyl L-methionine sER Smooth endoplasmic reticulum sn Stereospecific numbering snRNA Small nuclear ribonucleic acid THB Tetrahydrobiopterin THF Tetrahydrofolate TPP Thiamine diphosphate TRH Thyrotropin-releasing hormone (thyroliberin) tRNA Transfer ribonucleic acid TSH Thyroid-stimulating hormone (thyrotropin) UDP Uridine 5-diphosphate UMP Uridine 5-monophosphate UTP Uridine 5-triphosphate UV Ultraviolet radiation Vmax,V Maximal velocity(of an enzyme) VLDL Very-low-density lipoprotein 1.2 Terms 1. Acetyl CoA. 2. Actin. 3. Activated complex. 4. Active site. 5. Active transport. 6. Adenine. 7. Adenosine diphosphate 8. Adenosine triphosphate 9. Adenosine. 10. Adenylate cyclase. 11. Adipocyte. 12. Aerobe. 13. Afinity chromatography. 14. Alcohol. 15. Aldehyde. 16. Allosteric enzyme. 17. Amino Acid. 18. Anomers. 19. Antibody. 20. Anticodon. 21. Antigen. 22. Apoprotein 23. Asymmetric carbon. 24. ATP "Adenosine triphosphate". 25. Autoregulation. 26. B cell. 27. Beta-bend (-bend) or turn. 28. Beta-oxidation (-oxidation). 29. Beta-sheet (-sheet). 30. Bilayer. 31. Bile salts. 32. Bond energy. 33. Branchpoint. 34. Buffer. 35. cAMP. 36. Carbohydrate. 37. Carboxylic acid. 38. Carcinogen. 39. Carotenoids. 40. Catabolism. 41. Catalyst. 42. Catalytic site. 43. cDNA. 44. Cellulose. 45. Chelate. 46. Chemiosmotic coupling. 47. Chiral compound. 48. Chitin. 49. Chromatography. 50. Citric acid cycle. 51. Coactivator. 52. Coenzyme. 53. Cofactor. 54. Collagen. 55. Complementary base sequence. 56. Configuration. 57. Conformation. 58. Constitutive enzymes. 59. Cooperative binding. 60. Cytidine. 61. Cytochromes. 62. Cytokinin. 63. Cytosine. 64. De novo pathway. 65. Deamination. 66. Dehydrogenase. 67. Denaturation. 68. Dialysis. 69. Dimer. 70. Disulfide bridge. 71. DNA polymerase. 72. Deoxyribonucleic acid. 73. Domain. 74. Double helix. 75. Eicosanoid. 76. Electrophoresis. 77. Eluate. 78. Endergonic reaction. 79. Endocrine glands. 80. Endopeptidase. 81. Endoplasmic reticulum. 82. Enzyme. 83. Epimers 84. Ether. 85. Exergonic reaction. 86. Exon. 87. Exonuclease. 88. Fatty acid. 89. Feedback inhibition. 90. Fermentation. 91. Free energy. 92. Furanose. 93. Gel fitration chromatography. 94. Globular protein. 95. Gluconeogenesis. 96. Glucose. 97. Glycogen. 98. Glycogenic. 99. Glycolipid. 100. Glycolysis. 101. Glycoprotein. 102. Glycosidic bond. 103. Growth factor. 104. Guanine. 105. Guanosine. 106. Half-life. 107. Helix. 108. Heme. 109. Hemiacetal. 110. Hemoglobin. 111. Heteropolymer. 112. Hexose. 113. High-energy compound. 114. Histones. 115. Holoenzyme. 116. Homopolymer. 117. Hormone receptor. 118. Hormone. 119. Hydrogen bond. 120. Hydrolysis. 121. Hydrophilic. 122. Hydrophobic effect. 123. Hydrophobic. 124. Imine. 125. Immunoglobulin. 126. Induced fit. 127. Inducible proteins. 128. Interferon. 129. Isoelectric point or pH. 130. Isomerase. 131. Isomerization. 132. Ketogenic. 133. Ketone bodies. 134. Ketone. 135. Ketosis. 136. Kinase. 137. Krebs cycle. 138. Ligand. 139. Ligase. 140. Lipid bilayer. 141. Lyase. 142. Lysosome. 143. Membrane protein. 144. Membrane. 145. Messenger RNA (mRNA). 146. Micelle. 147. 148. 149. 150. 151. 152. 153. 154. 155. 156. 157. 158. 159. 160. 161. 162. 163. 164. 165. 166. 167. 168. 169. 170. 171. 172. 173. 174. 175. 176. 177. 178. 179. 180. 181. 182. 183. 184. 185. 186. 187. 188. 189. 190. 191. 192. 193. 194. 195. 196. 197. 198. Michaelis constant (Km). Mitochondrion. Monomer. Mutarotation. Myosin. Negative control. Nitrogen fixation. Nitrogenous base. . Noncompetitive inhibitor. Northern blotting. Nuclease. Nucleic Acid. Nucleic acids. Nucleophilic group. Nucleoside. Nucleotide. Oligosaccharide. Oncogene. Optical activity. Oxidation. Oxidative phosphorylation. Oxidoreductase. Pentose phosphate pathway. Pentose. Peptide. Peptidoglycan. Permeable. Peroxisomes. Phenylketonuria. Phosphate. Phosphodiester. Phospholipid. Pigment. Polar group.. Polyamine. Polymer. Polymerase. Polynucleotide phosphorylase. Polynucleotide. Polypeptide. Polysaccharide. Porphyrin. Posttranslational modification. Primary structure. Primer. Proprotein. Prostaglandin. Prosthetic group. Protamines. Protein subunit. Protein. Proteoglycan. 199. 200. 201. 202. 203. 204. 205. 206. 207. 208. 209. 210. 211. 212. 213. 214. 215. 216. 217. 218. 219. 220. Purine. Pyranose. Pyrimidine. Pyrophosphate. Regulatory enzyme. Renaturation. Ribose. Salting out. Salvage pathway. Second messenger. Secondary structure. Semipermeable. Southern blotting. Splicing. Starch. Stereoisomers. Steroids. Structural domain. Structural protein. Substrate. Subunit. Sugar. 1.3. 221. 222. 223. 224. 225. 226. 227. 228. 229. 230. 231. 232. 233. 234. 235. 236. 237. 238. 239. 240. 241. 242. TCA cycle. Terpenes. Tertiary structure. Tetramer. Thioester. Thymidine. Thymine. Transamination. Transcription. Transfer RNA Transferase. Transition state. Translation. Transport protein. Tricarboxylic acid cycle. Trypsin. Turnover number. Ultracentrifuge. Urea cycle. Vitamin. Zwitterion. Zymogen Guidelines for students Guidelines for students are published in the forms of academic manuals and textbooks 1) Laboratory Manual on Biochemistry. Part 1 Kuznetsova O.M., Berezov T.T., Chernov N.N. М.: DIGITPRESS. 2014. 58 P 2) Laboratory Manual on Biochemistry. Part 2 Kuznetsova O.M., Berezov T.T., Chernov N.N. М.: DIGITPRESS. 2015. 51 P 3) Collection of biochemistry tests. Berezov T.T., Chernov N.N. Kuznetsova O.M. M.: Изд-во «Оргсервис-2000». 2011, - 60 P. 1.4. Grade System Intermediate control (IC) includes written test (5 points) and computer test (5 points). The number of IC is 10 in accordance with the number of topics. Final examination is a written or computer test (100 points). Final mark is calculated according to the relation: IC (out of 100) + Final exam (out of 100)/ 2 = GRADING SCALE: Final grades will be based on the following scale: ECTS A B Traditional marks in the Russian Federation 5 Rating points Marks 95 - 100 86 - 94 5+ 5 C D E FX F 4 3 2 69 - 85 61 - 68 51 - 60 31 - 50 0 - 30 4 3+ 3 2+ 2 2. Examples of the questions for a self-examination and discussion in a class Topic 1 1. Asparagine contains the amide group 2. Protein molecules in solution are stabilyzed by electrical charge 3. Characteristic for cyclic amino acids is xanthoprotein reaction 4. The mixture of free amino acids gives the positive ninhydrin reaction 5. Precipitation of proteins from solution is more effective in Isoelectric point 6. Serine contains a free hydroxyl group 7. Valine, leucine and isoleucine possesse the hidrophobic properties 8. Are all proteins soluble in water? 9. Are the peptides bonds spleted during thermal denaturation of protein? 10. Does the mixture of free amino acids possess the positive biuret reaction? 11. Is the ornithine a component of native protein? 12. May the methionine be considered as derivatives of butyric acid? 13. Imidasol ring contains 1 nitrogen atom 14. N-Terminal amino acid in depeptide: Histidyl-Lysine is Histidine 15. C-Terminal amino acid in thripeptide: Serylprolylglycine is Glycine 16. Albumins of blood serum carry out the transport function 17. Proline contains the imino group 18. Aspartic acid is the derivatives of succinic acid 19. Do the all peptides give the positive biuret reaction? 20. Does the colour intensity of substance in solution depend from its concentration? Topic 2 1. Prostetic groups of nucleoproteins are represented by nucleic acids. 2. Carbohydrates could not be as prostetic group for complex proteins. 3. Phosphoric acid in phosphoproteins is joined through hydroxyl group of serine, threonine or tyrosine. 4. The minor bases more often meet (contain) in tRNA composition. 5. Protamines and histons are the component of nucleoproteins. 6. Myoglobin belongs to chromoproteins. 7. Are there differences in chemical structure of proteins and nucleic acids? 8. May be splited the hydrogen bonds during protein denaturation? 9. Are there nucleic acids the polynucleotides? 10. Are there distinguishes in quantity by carbon atoms in molecule of ribose and dexyribose? 11. The specificity of complex enzyme is determined by coenzyme. 12. The active site of enzyme consists from substrate binding and catalytic sector (site) 13. The enzyme activity do not depends from substrate concentration. 14. The enzymes catalyze both forward and revers reactions. 15. The velocity of enzyme reaction is always accelerated with the rise of pH medium. 16. The pepsin possesses with absolute specificity of action. 17. Is the enzyme-substrate complex always is formed during enzymatic reactions? 18. Does the velocity of enzymatic reaction depend from the enzyme concentration? 19. Does the ions of heavy metals influence on the enzyme activity? 20. May the enzymes be separated by ammonium sulfate precipitation? Topic 3 1. Carotine is the precursor of the vitamin A. 2. Vitamin E and K are the derivatives of sterols. 3. Vicasol is soluble in water. 4. Cobalt is the component of vitamin B 12. 5. Biotin (vitamin H) takes part in assimilation of carbon dixide by enzymes. 6. Vitamin B2 is the component of flavinmononucleotide (FMN). 7. Does the vitamin K takes part in the course of blood coagulation. 8. Are the known antivitamins of B1? 9. Is the vitamin B6 a component of coenzyme A? 10. Does the folic acid take part in the synthesis of purine nucleotides? 11. Lipids are hydrophilic compounds. 12. Palmitate and oleate have equal number of carbon atoms. 13. Cholesterides are the esters of cholesterol and higher fatty acids. 14. Hexose is a component of cerebrosides. 15. Cardiolipin belongs to glycerolipids. 16. To group of the licanosoids belongs: prostaglandins, prostacyclins, tromboxancs, and leucotrienes. 17. Hormons are able to regulate the activity of individual anzyme or enzyme systems. 18. Biological activity of hormons develops under very low of their concentration in blood. 19. Aldosteron belongs to glucocorticoids. 20. Vasopressin is the anterior pituitery hormon. Topic 4 1. 2. 3. 4. 5. 6. 7. The conversion of glucose into glycogen is called glycogenolysis Glycogen is a storage material. Glucose cannot enter the brain without insulin Glucagon secretion stimulates glycogenolysis. Gluconeogenesis is the conversion of glycogen to glucose Glucagon raises blood glucose Glyceraldehyde-3-phosphate dehydrogenase catalyzed step is the main step for energy yield under anaerobic conditions 8. Glycerol kinase is absent in the adipose tissues 9. Phosphoglycerate kinase catalyzed step yields energy by substrate level phosphorylation 10. Diabetic ketoacidosis is a commonest complication of type 2 diabetes mellitus 11. Insulin receptor has tyrosine kinase activity 12. Acetyl-CoA is an ideal substrate for gluconeogenesis 13. Insulin promotes lipolysis by stimulating hormone sensitive lipase 14. Oral glucose tolerance test is a confirmatory test in suspected case of diabetes mellitus 15. Aconitase enzyme catalyzes the condensation of Acetyl-CoA and oxaloacetate 16. Muscle glycogen functions to store and export glucose to maintain blood glucose between meals 17. Liver and kidney are the major gluconeogenic tissues 18. Glucose-6-phosphate dehydrogenase is an NAD+ dependent enzyme 19. Ribose cannot be synthesized in all tissues 20. The rate of TCA cycle is reduced when the cell has a high level of ATP Topic 5 1. Lipids are splited until free fatty acids. 2. Palmitate and oleate are the unsaturated compounds. 3. Chylomicrons are the transport forms of triacylglycerols. 4. 5. 6. 7. 8. 9. Glycerol is not a lipid. In the presence of bile lipase action is accelerated. The lipid acids activation is needed in energy spend. Does the carnitine takes part in fatty acids oxidation? May glycerol be transform into 3-phosphoglyceraldehyde in living cell? Does the preliminary activation of fatty acids needed for the biosynthesis of neutral lipids? 10. May the proteins be splited under lipase action? 11. In β-oxidation of fatty acids take part FAD-, and NAD-dependent dehydrogenases. 12. The complete oxidation of 1 mole of palmitate till CO2 and H2 O is accompaned with formation of 130 molecules of ATP. 13. Linolenic acid is essential for human. 14. Mevalonic acid synthesis is needed in the presence of NADP·H2 . 15. Prostaglandins are synthesized from polyansaturated futty acids 16. Cholesterol in blood serum exist only in free state. 17. May NADP·H2 be changed or substituted by NAD·H2 in the cours of higher fatty acid synthesis? 18. Takes the biotin part in the fatty acids synthesis? 19. Is the complete convertion of neutral lipids into carbohydrates possible in animal organisms? 20. Are there all stages of β-oxidations of fatty acids reversible in mitochondria? Topic 6 1. 2. 3. 4. Proteinases, amylases and lipases belong to class of hydrolase. Taurine is the metabolite product of cysteine. Scatol and indol are formed in intestine from amino acid tyrosine. Hydrochloric acid in stomach activates the pepsinogen. 5. During deamination of amino acids in organism the biogenic amines are formed. 6. 7. 9. Tyrosine is the essential amino acid for human. Different coenzymes may take part in oxidative deamination of amino acid. The transamination reactions of amino acids are irreversible. -Ketoglutarate takes part in both transdeamination and transreamination of amino acids. 10. FAD is the coenzyme for aminotransferases. 11. In the course of transamination ammonia is liberated. 12. Is the convention of pyruvate into alanine possible in organism of human? 13. Is the phenylalanine a precursor for serotonin? 14. May the determination of aspartate amino transferase activity in blood serum be used for diagnosis of heart infarction? 15. Is the vitamin B1 needed for transamination reaction? 16. Histidine in liver may deaminate by the mechanism of intramolecular deamination. 17. The reduced coenzymes of amino acid oxidases may directly oxidated by molecular oxygen. 18. Glutamate deamination occurs through intermediate formation of imino acid. 19. FAD is the coenzyme for monoaminoxidases (MAO). 20. Decarboxylation of amino acids is the irreversible processes. Topic 7 1. Amide nitrogen of glutamine may be used for heme synthesis. 2. Heme synthesis takes place in cell cytosol. 3. Acetyl-CoA is necessary for heme synthesis. 4. The direct bilirubin is mono- or diglucuronide of biliribin. 5. Indirect bilirubin inters into bile stones. 6. Iron for heme synthesis stores in the form of ferritin. 7. Does the heme synthesis regulated by the feedback type? 8. Is the δ-aminolevulinate synthase an allosteric enzyme? 9. Is the stercobilinogen formed in liver? 10. Is the bilirubin colored? 11. The nitrogen compounds of food are used for nucleic acid synthesis of our organism. 12. Glutamate is precursor of NH2 –group for GMP synthesis from imosinic acid. 13. The end product of adenosine degradation in human is uric acid. 14. The normal value of uric acid concentration in human blood is 0.2 g/l. 15. The regulation of pyrimidine bases is realized by the type of feed-back. 16. The nitrogen of pyrimidine bases is rexcreted from organism in the form or urea in general. 17. Takes the asparagine part in the synthesis of purine ring? 18. May the CMP be synthesized from UMP? 19. Is the β–alanine the end product of TMP catabolism in human organism? 20. Takes the carbamoylphosphate part in the synthesis of pyrimidine nucleotides? 3. Tasks for an individual work Topic 1 1. 2. 3. 4. 5. 6. 7. 8. 9. Amino acids: their structure and properties. Classification of the amino acids. Essential and nonessential amino acids. Polypeptide chain. The ways of natural peptides synthesis. Examples of natural peptides: oxytocin, vasopressin, angiotensin, glutathione. Structural features of the peptides, providing their resistance to proteolysis. Amino acid composition of proteins. Color reactions of proteins. Levels of protein structure: primary, secondary, tertiary and quaternary structure. 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, 7dehydrocholesterol. 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 1. 3. 4. 5. 6. 7. 8. 9. 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 Peculiarities of absorption and transport of lipids. Degradation and synthesis of triacylglycerols. Oxidation of glycerol. -oxidation of fatty acid in mitochondria Biosynthesis of fatty acids and phospholipids in different tissues. Acetone bodies. Biosynthesis of cholesterol 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. 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. Digestion of proteins in gastrointestinal system. Absorption and active transport of amino acids. Protein putrefaction in the intestine (indole, skatole, phenol, cresol) 2. Pathways of amino acid metabolism. Deamination (oxidative and non-oxidative) and transamination of amino acids. Role of the coenzymes in these reactions. Diagnostic significance of the aminotransferases in the blood 3. The fate of α-keto acids. Glucogenic and ketogenic amino acids. 4. Synthesis and degradation of biogenic amines and their biological role. MAO 5. Notion on hydroxylation and methylation reaction. (Examples) 6. The ammonia detoxification pathways. Urea synthesis in the liver. 7. Metabolism of individual amino acids: a. Gly, Ser, b. Cys, Met, c. Arg, d. Glu, Asp, e. Phe, Tyr, Trp 8. Biosynthesis of creatine phosphate and its physiological role. 9. Regulation and pathology of amino acids metabolism. Topic 7 1. Sources of purine nucleus 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 the direct and indirect bilirubin in the blood serum. 7. Protein biosynthesis. The main components of the protein synthesis system. Posttranslational 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 others) 10. Abnormal urine components. 11. Basic nitrogen-containing inorganic components of the urine. 12. The main chemical components of human serum. Examples of the tests Amino Acids and Simple Proteins 1 Essential for man amino acids are: 1 Phenylalanine 2 Tyrosine 3 Tryptophan 4 Threonine 5 Histidine 2 Which from the following amino acids have the positive charge? 1 Asparagine 2 Glutamine 3 Lysine 4 Glutamate 5 Histidine 3 Sulphur containing amino acids are: 1 Methionine 2 Lysine 3 Valine 4 Cysteine 5 Arginine 4 Hydrophobic amino acids are: 1 Glutamine 2 Valine 3 Threonine 4 Phenylalanine 5 Isoleucine 5 Which from the following bonds do not break during protein denaturation? 1 Disulphides 2 Hydrogens 3 Peptides 4 Ionics 5 Hydrophobics 6 The donator of methyl groups is: 1 Valine 2 Leucine 3 Methionine 4 Arginine 5 Threonine 7 The largest value of Rf for amino acid during paper chromatography is for: 1 Glycine 8 9 10 11 2 Threonine 3 Serine 4 Glutamate 5 Valine The isoelectric point of proteins depends on the presence of: 1 Hydrate layer 2 Total charge 3 Hydrogen bonds 4 Helical parts in protein molecule 5 All of the above The biuret reaction is positive for: 1 Simple proteins 2 Dipeptides 3 Tripeptides 4 Solution of amino acids 5 Gelatine The main property of the oligomeric proteins: Penetrate through semipermeabile 1 membrane 2 Do not contain α-helical regions 3 Consist from several polypeptide chains 4 Do not possess the tertiary structure 5 All of the above Hydrophilic amino acids are: 1 Glutamine 2 Serine 3 Arginine 4 Phen 5 l a l a Asparagine n i n e 12 Amino acid without stereoisomeres is: 1 Tyrosine 13 14 15 16 17 18 19 2 Glysine 3 Alanine 4 Cysteine 5 Serine Essential for man amino acids are: 20 1 Lysine 2 Threonine 3 Ornithine 4 Valine 5 Cysteine Amino acids which are the derivatives of propionic acid: 21 1 Alanine 2 Serine 3 Cysteine 4 Threonine 5 Phenylalanine Hydrophobic amino acid is: 22 1 Serine 2 Leucine 3 Glutamine 4 Cysteine 5 Lysine Protein denaturation may be achieved by: 23 1 Concentrated nitric acid 2 Copper sulphate 3 Silver nitrate 4 Concentrated alkaline 5 Ammonium sulphate 24 The amino acid with thiol group is: 1 Aspargine 2 Histidine 3 Lysine 4 Cysteine 5 Metionine Which pairs of the following amino acids 25 can not be separated by ion-exchange chromatography? 1 Glutamate and Lysine 2 Glutamate and Leucine 3 Leucine and Lysine 4 Leucine and Valine 26 5 Valine and Glutamate The denaturation of proteins always accompany with the: 1 Destruction of tertiary structure 2 Hydrolysis of peptide bonds 3 Appearance of color Formation of functional complexes with 4 other proteins Elimination of native biological 5 properties Which of the following bonds stabilize the tertiary protein structure? 1 Esters 2 Hydrophobics 3 Hydrogens 4 Ions 5 Disulphides The ninhydrin reaction is negative with: 1 Simple proteines 2 Dipeptides 3 Tripeptides 4 Free amino acids 5 Carbonic acids Collagen contains the largest amount of amino acid residues: 1 Histidine 2 Glycine 3 Asparagine 4 Leucine 5 Glutamate Glutathione is a: 1 Amino acid 2 Dipeptide 3 Ttripeptide 4 Tetrapeptide The derivative of succinate is: 1 Glutamate 2 Histidine 3 Proline 4 Tryptophan 5 Aspartate Molecular mass of proteins may be determined by: 1 Sedimentation analysis 2 Dialysis 3 Ion-exchange chromatography 4 Colorimetry 5 Gel-filtration Albumines are soluble in: 1 Distilled water 2 Phosphate buffer, pH=6.8 3 Semisaturated ammonium sulphate 4 Semisaturated copper sulphate 5 Saturated ammonium sulphate 2 Primary structure of nucleic acids 3 Tertiary structure of proteins 27 The mixture of proteins with different molecular masses may be separated by: 4 Tertiary structure of nucleic acids 1 Gel-filtration 30 Hydrophilic amino acids are: Ultrafiltration through the filter with 1 Phenylalanine 2 different size of pores 2 Leucine 3 Dialyses 3 Threonine 4 Ultracentrifugation 4 Serine 5 Salting-out 5 Alanine 28 The positive xanthoprotein reaction is typical for: 1 Phenylalanine 2 Methionine 3 Tryptophan 4 Arginine 5 Asparagine 29 Shaperons take part mainly in the formation and stabilization of: 1 Primary structure of proteins Conjugated Proteins, Nucleic Acids and Enzymes 1 Amylase belongs to the following class of 3 Pyrimidine Enzymes: 4 Imidasole 1 Oxidoreductases 5 Pyridine 2 Hydrolases 6 The enzyme may be activated by: 3 Lyases 1 Substrate 4 Ligases 2 Allosteric inhibitor 5 Isomerases 3 Product of reaction 2 The Enzyme mixture can not be 4 Cofactor separated by: 7 The specific activity of an enzyme means: 1 Precipitation 1 The amount of enzyme that produces 1 2 Dialysis mol of product per second under 3 Gel Filtration standard conditions 4 El 2 The activity of an enzyme in relation to a standard preparation of the enzyme 5 3 The number of enzyme units per c milligram of protein tr 4 The amount of enzyme causing o transformation of 1 μmol of substrate per p minute under standard conditionss h 5 The activity of an enzyme in the o presence of its preferred substrate r e 8 An enzyme that catalyzes the synthesis of si organic substances using ATP hydrolisis s would be classified as: 1 Oxidoreductases on-Exchange Chromatography 2 Transferases 3 Hydrolases 3 The Enzyme catalyzing interconversion of ketoses and aldoses belongs to the class 4 Isomerases 5 Ligases of: 9 Enzymes increase the rates of reactions 1 Oxidoreductases by: 2 Transferases 1 Increasing the free energy of activation 3 Hydrolases Increasing the free-energy change of the 4 Isomerases 2 reaction 5 Lyases 4 Cholinesterase catalyses the hydrolysis of 3 Changing the equilibrium constant of the reaction bonds: 4 Decreasing the energy of activation 1 Ester 10 The Michaelis constant (KM) is: 2 Glucosides 1 Numerically equal to Vmax/2 3 Peptides The equilibrium constant for the 4 Disulfides 2 dissociation of ES to E + P 5 Hydrogens Increased at the presence of non5 Heme molecule consist from four 3 competitive inhibitor derivatives of rings: The substrate concentration at which V 1 Pyrrole 4 is one-half of Vmax 2 Purine 11 Which of the following regulatory actions involves a reversible covalent modification of an enzyme? 1 Allosteric modulation 2 Competitive inhibition 18 Conversion of zymogen to active 3 enzyme Association of apoenzyme with a 4 cofactor Phosphorylation of the hydroxyl group in 5 the serine residues 19 12 The type of enzyme inhibition in which KM increases but Vmax does not change is: 1 Competitive 2 Non-competitive 3 Irreversible 4 Uncompetitive 13 An allosteric effector changes the enzyme activity by: Competing for the catalytic site with the 1 substrate Binding to a site on the enzyme molecule 2 20 distinct from the catalytic site 3 Precipitating of the enzyme molecule 4 None of the above 14 Catalase belongs to the class of enzymes: 1 Oxidoreductases 2 Transferases 21 3 Hydrolases 4 Lyases 5 Isomerases 15 … does not bind to the active site of enzyme: 1 Substrate 2 Product 22 3 Coenzyme 4 Competitive inhibitor 5 Allosteric effector 16 The subunit number in lactate dehydrogenase: 1 2 3 4 5 Two Three Four Six Eight 17 Kinases require: 1 Mn 2 Cu 3 Mg Inorganic 4 phosphate 5 Zinc Apoenzyme may be activated by: 1 Substrate 2 Allosteric activator 3 Product of reaction 4 Coenzyme One enzyme unit means: 1Quantity of enzyme which catalyzes the formation of 1 mole of the product per second Quantity of moles of the substrate, 2 undergo by 1 mol of enzyme per sec Number of Enzyme units per 1 mg of 3 protein 4Quantity of enzyme which catalyze the formation of 1 micromole of the product per minute 5 Activity of enzyme to the best substrate Сompetitive inhibitors: 1 Increase the KM enzyme 2 Decrease the KM enzyme 3 Increase Vmax 4 Decrease Vmax 5 Do not change KM and Vmax Specificity of Holoenzyme depends from: 1 Coenzyme 2 Apoenzyme 3 Allosteric effector 4 Cosubstrate 5 All indicated factors Which enzyme does not belong to Oxidoreductases: 1 Catalase 2 Peroxidase 3 Cholinesterase 4 Ascorbate oxidase 5 Lactate dehydrogenase 23 Enzymatic Reaction rate accelerates by: 1 Decreasing the temperature 2 Increasing the enzyme quantity 3 Denaturation of enzyme 4 Coenzyme deficiency 5 Edition of allosteric activator 24 The substance with the catalytical activity is: groups in enzyme 1 Insulin 3 Change of substrates charge 2 Glucagon 4 Dissociation of enzyme 3 Casein 5 Denaturatin of enzyme 4 Pepsin 29 If the substrate concentration is equal to 5 Keratin KM the reaction rate may be: 1 0.25 Vmax 25 Сompetitive inhibition may be reversed by: 2 0.33 Vmax 1 Rising the temperature 3 0.50 Vmax 2 Adding the product of reaction 4 0.67 Vmax 3 Excessive substrate concentration 5 0.75 Vmax 4 Heav 30 Which proteins take part in a specific metal ions links and transport of iron? 1 γ-Globulins 26 Enzyme which belongs to 2 α-Globulins Oxidoreductases: 3 Transferrins 1 Amylase 4 Ceruloplasmin 2 Tripsin 5 Albumins 3 Catalase 4 Cholinesterase 5 Pepsin 27 It is not Hemoprotein: 1 Myoglobin 2 Cytochrome c 3 Catalase 4 Hemoglobin 5 Casein 28 Changes of pH medium may lead to: Break of peptide bonds in enzyme 1 molecule 2 Change of ionization of dissociated Vitamins, Lipids and Hormones 1 The causes of hypovitaminoses may be due to: 1 Deficiency of vitamin in food 2 Disturbance of vitamin transport 3 Disturbance of coenzyme synthesis 4 Genetic defect of apoenzyme 2 The vitamin with the maximum daily requirement for human is: 1А 2 В1 3 РР 4D 5Е 3 The vitamins with heterocycles in their structure are: 1 Tocopherol 2 Thiamine 3 Pyridoxine 4 Niacin 5 Pantothenic acid 4 The vitamins which are essential for hydrogen transport: 1 Thiamine 2 Riboflavin 3 Folic ac 4 d Niacin 8 9 10 11 5 Biotin 5 The vitamin which is the component of coenzyme A is: 12 1 Thiamine 2 Riboflavin 3 Pantothenic acid 4 Pyridoxine 5 Cobalamin 6 The characteristic symptom of Vitamin PP deficiency: 13 1 Sclerosis 2 Rickets 3 Pellagra 4 Scurvy 5 Beriberi 7 Coenzyme is attached to enzyme: 14 1 In allosteric centre 2 Always in active site 3 By different chemical bounds 4 Tightly or not tightly Gs-protein: 1 Contains three subunits 2 Is connected with GDP or GTP 3 Inhibits adenylate cyclase 4 Is a membrane protein 5 Activates DNA The vitamin D deficiency in adults may cause: 1 Osteomalacia 2 Xerophtalmia 3 Macrocytic anemia 4 Scurvy 5 Rickets The Vitamins which do not contain the heterocycles in their structure are: 1 Retinol 2 Pyridoxine 3 Cholecalciferol 4 Riboflavin 5 All indicated vitamins The vitamin with the minimal daily requirements for human is: 1A 2D 3C 4 PP 5E The vitamin which is essential for NH2group transfer is: 1 Pyridoxine 2 Riboflavin 3 Thiamine 4 Ascorbic acid 5 Nicotinamide Steroid hormones: 1 Penetrate into the cell 2 Bind with membrane receptors 3 Activate G-protein 4 Stimulate the mRNA synthesis 5 Participate in all indicated processes NAD+ and NADP+ are coenzymes of vitamin: 15 16 17 18 19 20 21 1P 2 PP 3K 22 4C 5 B3 The vitamins with antioxidant activity are: 1Н 2 В6 3А 23 4Е 5С Adenylatcyclase is: 1 A membrane enzyme 2 A cytoplasmic enzyme 24 3 Activated by Gs-protein The enzyme which catalyzes the cAMP 4 synthesis 5 Containing heme Which substance is a nucleotide? 1 Adenine 2 Adenine hydrolase 3 Cytidine 25 4 Prion Adenosine 5 monophosphate Essential fatty acids are: 1 Linoleic acid 2 Linolenic acid 26 3 Arachidonic acid 4 Oleic acid 5 Palmitic acid Fat-soluble vitamins are: 1 Pyridoxine 27 2 Thyamine 3 Retinol 4 Philloquinone 5 Folic acid Saturated fatty acid is: 1 Oleic acid 28 2 Linoleic acid 3 Linolenic acid 4 Palmitic acid 5 Arachidonic acid Coenzyme of succinate dehydrogenase is: 1 NAD+ 2 FAD 29 3 FMN 4 TPP 5 CoA The requirement of what vitamin is rising with aging and hard working? 1 B1 2 B2 3 B3 4 B6 5 B12 Which pair of vitamins contains sulfur atom in their molecules? 1 Thiamine and Biotin 2 Thiamine and Folic acid 3 Pyridoxine and Biotin 4 Biotin and Riboflavin Vitamin which is required for carboxylation reaction is: 1 Thiamine 2 Biotin 3 Cobalamin 4 Pyridoxine 5 Ascorbic acid Water-soluble vitamins are: 1 Retinol 2 Niacin 3 Cobalamin 4 Tocopheroll 5 Biotin Nitric oxide(NO) is: 1 Bioactive molecule 2 Synthesized from lysine 3 Synthesized from arginine 4 Exert long effect The steroid derivatives are: 1 Sex hormones 2 Glucocorticoids 3 Bile pigments 4 Cholesterol 5 All indicated substances FAD and FMN are coenzymes of vitamin: 1 B1 2 B2 3 B3 4 B6 5 B12 Which chemical substances are not a component of biomembrane: 1 Glycerol 2 Cholesterol 3 Sphingomyelins 4 Phosphatidylcholines 5 Triacylglycerols 30 Calmodulin is: 1 Glycerophspholipid 2 Thyroid hormone 3 Intracellular Ca2+-binding protein 4 Precursor of calcitonine 5 No one from indicated substances 2 12 3 38 Chemistry and Metabolism of 4 15 Carbohydrates 5 72 8 The main function of pentose phosphate 1 Normal Glucose level in blood serum is: pathway in erythrocyte is: 1 3.3-5.5 mmol/l 1 Synthesis of NADPH++H+ 2 2.2-2.3 mmol/l 2 Synthesis of xylulose-5-phosphate 3 5.5-8.6 mmol/l 3 Splitting of pentose phosphates 4 2.0-6.6 mmol/l 4 Synthesis of ATP 5 10.5-11.0 mmol/l 5 Reduction of H2O2 to H2O 2 The end product of anaerobic glycolysis 9 Noninsulin-dependent Diabetes Mellitus in muscle is: occurs due to: 1 Pyruvate 1 Alteration of glycolysis regulation 2 Lactate 2 Increasing of insulin secretion 3 Oxaloacetate 3 Increasing of glucagon secretion 4 Ethanol 4 Decreasing of insulin secretion 5 Acetyl-CoA 5 Changes of insulin-dependent uptake of glucose 3 Normal values of glucose in blood serum10 are:The common stage of glycolysis 1 3-5 g/l and gluconeogenesis, catalyzed 2 0.6-1.0 g/l by common enzyme is: 3 3.3-5.5 mmol/l 1 Fru-6-ph Glc-6-ph 4 60-100 mg/dl 2 Glc-6-ph Glc 5 None from indicated 3 Oxaloacetate Phosphoenolpyruvate 4 The content of pyruvate in blood 4 Fru-1,6-bisph Fru-6-ph is raised during the hypovitaminosis: 5 No one from indicated 1 A 11 The Enzyme which does not take part in CAC: 2 C 1 Aconitate hydratase 3 D 2 Transketolase 4 B1 3 Succinate dehydrogenase 5 B6 4 Fumarate hydratase 5 The Enzyme which limits the rate 5 Malate dehydrogenase of glycolysis is: 12 Which enzymes of glycolysis catalyse 1 Glyceraldehyde phosphate dehydrogenase the irreversible reactions? 2 Enolase 1 Thriosophosphate isomerase 3 Phosphofructokinase 2 Aldolase 4 Phosphoglycerate kinase 3 Phosphofructokinase 5 Triosophosphate isomerase 4 Lactate dehydrogenase 6 Which products may be formed 5 Hexokinase from Glucose-6-phosphate in one stage? 13 Lactose is degraded to: 1 Fructose-6-phosphate 1 Galactose and glucose 2 Glucose 2 Galactose and fructose 3 6-Phosphoglucone lactone 3 Glucose and mannose 4 Glucose-1-phosphate 4 Glucose and fructose 5 Fructose-1-phosphate 5 Only Glucose 7 The energetic value (ATP quantity) 14 Maltose is degraded to: of pyruvate oxidation to CO2 and H2O: 1 Galactose and glucose 1 24 2 Galactose and fructose 15 16 17 18 19 20 21 3 Glucose and mannose 4 Glucose and fructose 5 Only Glucose 22 Sucrose may be splited only in: 1 Brain 2 Liver 3 Muscle 4 Intestine 5 Kidney 23 Which monosaccharide is formed during full hydrolysis of glycogen? 1 D-Fructose 2 Fructose-6-phosphate 3 Glucose-6- phosphate 4 D-Glucose 5 Fructose-1,6-bisphosphate 24 In which C-atom of pyruvate 14 will appeared C-1 of Glucose? 1 1 2 2 3 3 4 In all atoms 5 None of atoms 25 The substrate phosphorylation takes place in the course of: 1 Glycolysis 2 Gluconeogenesis 3 Glycogenolysis 4 Pentose Phosphate pathway 5 CAC 26 The major quantity of Glycogen in the organism is in: 1 Liver 2 Muscles 3 Brain 4 Kidney 27 5 Adipose tissue Which substances are allosteric regulators? 1 AMP 2 ATP 3 Fructose-6-phosphate 4 Citrate 28 5 Pyruvate In which reaction of CAC the hydratation is occurs? 1 α-Ketogutarate Succinyl-CoA 2 L-Malate Oxaloacetate 3 Succinate Fumarate 4 Fumarate L-Malate 5 Isocitrate α-Ketoglutarate Which metabolic pathways supply the sugars for nucleic acid synthesis? 1 Glycolysis 2 Gluconeogenesis 3 Glycogenolysis 4 CAC 5 Penthose Phosphate pathway In patients with diabetes the hyperdose of insulin may lead to: 1 Glucosuria 2 Galactosemia 3 Hyperglycemia 4 Hypoglycemia 5 Creatinuria Which enzyme participates in the formation of Glucose-1-phosphate from glycogen? 1 Amylase 2 Phosphorylase 3 Phosphoglucoisomerase 4 Phosphoglucomutase 5 Glucokinase The net yield of ATP during CAC (without oxidative phosphorilation) is: 1 0 2 1 3 2 4 38 5 12 Glucose may be formed in the organism from: 1 Acetyl-CoA 2 Pyruvate 3 Lactate 4 Glycerol Enzymes which catalyze the glycogen synthesis from glucose are: 1 Amylase 2 Phosphorylase 3 Glycogen synthase 4 Phosphoglucomutase 5 Glucokinase The rate of glycolysis in muscle is diminished in the presence of: 1 ADP 2 ATP 3 Citrate 4 AMP 29 The products which are formed from Pyruvate in one step are: 1 Citrate 2 Oxaloacetate 3 Lactate 4 Acetyl-CoA 5 Glycerol 30 Enzyme which is present both in liver and in muscle is: 1 Glucose-6-phosphatase 2 Hexokinase 3 Fructose-1,6-bisphosphatase 4 Pyruvate carboxylase 5 Glucokinase Lipid metabolism 1 Saturated fatty acids are: 1 Oleic 2 Arachic 3 Palmitoleic 4 Palmitic 5 Arachidonic 2 Which of the following substances are the derivatives of cholesterol? 1 Vitamin D3 2 Vitamin A 3 Bile acids 4 Corticosteroids 5 Prostaglandins 3 Unsaturated fatty acids are: 1 Palmitic 2 Oleic 3 Stearic 4 Arachic 5 Arachidonic 4 The allosteric enzyme which regulates the fatty acids synthesis in cytosol: 1 Acetyl-CoA carboxylase 2 Hexokinase 3 Phosphofructokinase 4 Citrate synthase NADP +-dependent β-hydroxy- β5 methylglutaryl-CoA 8 9 10 11 eductase 5 The content of triacylglycerols in chylomicrons (in %) is approximately: 1 10 2 20 3 30 4 50 5 80 6 Which substance participates in fatty acids transport from cytosol into mitochondria? 1 Ornithine 2 Carnitine 3 Taurine 4 Creatine 5 Albumin 7 The participants in the biosynthesis of 12 13 fatty acids are: 1 Carnitine 2 Biotin 3 Sphingosine 4 Cerulopasmin 5 NADPH(H+) Which substance participates in phosphatidylserine synthesis? 1 Lecithin 2 CDP-diacylglycerol 3 Leucine 4 S-Adenosylmethionine 5 Sphingosine Which substances are the components of biomembrains? 1 Diacylglycerol 2 Free fatty acids 3 Cholesterol 4 Phospholipids 5 Glycolipids Recirculation between liver and intestine is typical for: 1 Phospholipids 2 Monoacylglycerols 3 Glycerol 4 Lysophospholipids 5 Bile acids The antiatherogenic property is typical for: 1 Chilomicrons 2 HDL 3 LDL 4 VLDL 5 Cholesterol esters In mitochondria takes place: 1 The fatty acid β-oxidation 2 Citrate synthesis 3 Triacylglycerol lipolysis 4 Phospholipids biosynthesis 5 Synthesis of ketone bodies Eicosanoids are formed from arachidonic acid through: 1 Isomerisation 2 Methylation 3 Decarboxylation Entherocytes? 4 Carboxylation and hydrolysis Cyclooxygenase and lipoxygenase 1Triacylglycerols 5 pathways 2 Fatty acids 14 The triacylglycerols lipolysis in the fat 3 Bile acids tissue is inhibited by: Ketone 4 1 Insulin and Prostaglandins bodies 2 Catecholamines Phospholipid 5 s 3 Mineralcorticoids 21 The main metabolic pathway of fatty 4 Glucocorticoids acids in tissues is: 5 Glucagon 1 Chylomicron biosynthesis 15 The ketone bodies synthesis takes place 2 β-Oxdation in: 3 Lipid transport 1Cytosol 4 Cell membranes construction 2 Mitochondria 5 Binding of metal ions 3 Nucleus 22 Acetyl-CoA carboxylase is inhibited by: Goldgy 4 1 Citrate complex 2 ATP 5 Microsomes 3 Mn2+ 16 The substances which are the most active 4 Palmitic asid in fat emulsification in intestine: 5 Biotin Bile acids salts, unsaturated fatty acids 1 Substances that inhibit the lipolysis in fat tissue are: 23 and monoacylglycerols 1 Thyroid hormones 2 Bile pigments and bile acids 2 Insulin, Prostaglandins 3 Organic and mineral acids 3 ACTH, Somatotropin 4 Cholesterol and steroid hormones 4 Catecholamines 5 Fat-soluble vitamins 5 Glucocorticoids 17 The coenzymes that take part in β24 The ketone bodies are: oxidation of fatty acids are: + 1 Acetyl-CoA, Succinyl-CoA 1 NAD + 2 Acetoacetate, β-hydroxybutyrate 2 NADP 3 Acetoacetyl-CoA, Propionyl-CoA 3 FAD 4 Fumarate,Pyruvate, Malate 4 Coenzyme A 5 Oleate, Palmitate, Stearate 5 THF 18 To the group of Eicosanoids belong: 25 Acetyl-CoA takes part in the synthesis 1 Prostaglandins of: 2 Prostacyclins 1 Glycerol 3 Thromboxanes 2 Cholesterol 4 Leucotrienes 3 Pyruvate 5 Isoprenoids 4 Acetoacetate 19 Which substance takes part in 5 Fatty acids phosphatidylcholine biosynthesis by 26 The coenzyme which is essential for methylation reaction? biosythesis of cholesterol and fatty acids 1 Cholesterol is: 2 B12 1 NADH(H+) 3 S-Adenosylmethionine 2 FADH2 4 Biotin 3 NADPH(H+) 5 N5-Methyl-THF 4 Vitamin H (Biotin) 20 Which substances are resynthesized in 5 Pyridoxal phosphate 4 Thyroxin, Glucocorticoids 5 Hypothalamic hormones 27 Succinyl-CoA is formed in the course of: 1 Fatty acid β-oxidation 30 Which substance acts as allosteric activator in fatty acid synthesis? 2 Arachidonic acid oxidation 1 NADPH(H+) 3 CAC 2 Palmitic acid 4 Fatty acid biosynthesis 3 CO2 5 Sphingolipid biosynthesis 4 Citrate 28 The precursor of Eicosanoids is: 5 Avidin 1 Palmitate 2 Arachinate 3 Arachidonate 4 Stearate 5 Oleate 29 Hormones that activate the lipase in adipocytes are: 1 Adrenaline, Noradrenaline 2 Prostaglandins, Insulin 3 Oxytocin, Vasopressin Amino acid metabolism 1 The amino acid which participates in detoxification of ammonia is: 1 Histidine 2 Asparagine 3 Glutamate 4 Glycine 5 Tryptophan 2 The coenzyme of glutamate dehydrogenase is: 1 НАД+ 2 Pyridoxal phosphate 3 FAD 4 FMN 5 Coenzyme Q 3 Phenylketonuria is developed due to enzyme deficiency of classes: Supply the synthesis of biological amines 2 Demands the participation of PLP 3 Supply the essential amino acid synthesis 4 Is the ammonia liberation reaction Leads to the elevation of amino acid 5 levels in tissue The substances which do not participate in urea formation cycle are: 1 Citrulline 2 Ornithine 3 Succinate 4 Arginine 5 Asparagine To mixture (both ketogenic and glucogenic) amino acids belong: 1 Alanine 2 Glycine 3 Phenylalanine 4 Serine 5 Leucine Tetrahydrofolate participates in the synthesis of: 1 Serine from Glycine 2 Citrulline from Ornithine 3 Tyrosine from Phenylalanine 4 Glutamate from Hisidine 5 Glutamine from Glutamate Amino acids which do not participate in transamination reaction are: 1 Glutamine and Asparagine 2 Lysine and Threonine 3 Isoleucine and Tyrosine 4 Phenylalanine and Tyrosine 5 Alanine and Valine The NH3 in brain tissues is neutralized through: 1 Synthesis of urea 2 Formation of NH4Cl 3 Convertion of Glutamate to Glutamine 4 Alanine formation 5 Creatine synthesis The coenzyme of majority amino acid decarboxylases is: 1 FAD 1 8 9 1Oxidoreductases 2 Transferases 3 Hydrolyses 4 Lyases 5 Isomerases 4 The daily excretion of creatinine in urine 10 is: 1 0.1-0.2 g 2 1.0-2.0 g 3 10-20 g 4 1.0-2.0 mg 5 10-20 mg 5 Inherited deficiency of the homogentisate 11 1,2-dioxygenase leads to the development of: 1 Phenylketonuria 2 Parkinsone disease 3 Alkaptonuria 4 Albinism 12 5 Homocystinuria 6 Which amino acid participates in creatine synthesis? 1 Valine 2 Leucine 3 Methionine 4 Serine 13 5 Threonine 7 The process of amino acid transamination: 14 15 16 17 18 19 20 2 FMN 3 Pyridoxal phosphate 4 TPP 5 Biotin Histidase belongs to the class of enzyme: 1 Oxidoreductases 2 Transferases 3 Hydrolases 4 Lyases 5 Isomerases Skatole and Indole are formed by intestinal microflora action from: 1 Tyrosine 2 Triptophan 3 Histidine 4 Phenylalanine 5 Proline Pyridoxal phosphate is a coenzyme of: 1 Alanine aminotransferase 2 Glycogen phosphorylase 3 Aspartate aminotransferase 4 Amino acid Decarboxylase The CAC metabolite which participates in transamination reaction is: 1 Citrate 2 Isocitrate 3 Succinate 4 Fumarate 5 Oxaloacetate γ-aminobutirate is formed from: 1 Histidine 2 Aspartate 3 Glutamate 4 Glutamine 5 Asparagine The normal human urea value in daily urine is: 1 25-35 mg 2 0.25-0.35 g 3 2.5-3.5 g 4 25-35 g 5 250-350 g Glycine may be formed from: 1 Methionine 2 Lysine 3 Valine 4 Tyrosine 21 22 23 24 25 26 27 5 Serine Nitric oxide (II) is formed from: 1 Arg 2 Cys 3 Val 4 His 5 Ser Albinism is connected with the abnormal metabolism of: 1 Methionine 2 Serine 3 Cysteine 4 Tyrosine 5 Tryptophan The coenzyme of L- amino acid oxidase is: 1 FMN 2 Pyridoxal phosphate 3 NAD+ 4 NADP+ 5 CoA The activity of aspartate aminotransferase in blood serum is suddenly increased under: 1 Myocardial infarction 2 Pancreatities 3 Prostatities 4 Nephrites 5 Stomach diseases HCl in Stomach participates in: 1 Protein denaturation 2 Antibacterial action 3 Activation of pepsinogen Providing of an optimal pH medium for 4 pepsin action 5 Inhibition of pepsinogen Coenzyme of monoamine oxidase (MAO) is: 1 NAD+ 2 FAD 3 NADH(H+) 4 TPP 5 Pyridoxal phosphate Kwashiorkor (a children disease) is observed during the deficiency in food: 1 Carbohydrates 2 Lipids 3 Proteins 4 Vitamins 5 Inorganic substances 28 Taurine is formed from: 1 Leucine 2 Cysteine 3 Glycine 4 Serine 5 Threonine 29 Ketogenic amino acid is: 1 Leucine 2 Cysteine 3 Alanine 4 Glycine 5 Threonine 30 Monooxygenases participate in the synthesis of: 1 Tyrosine Dihydroxyphenylalani 2 ne 3 Noradrenaline 4 5-Hydroxytryptophan 5 Asparagine Synthesis of protein, DNA, RNA. Metabolism of Conjugated Proteins 1 The elevation of alkaline phosphatase activity in plasma takes place during pathology of tissues: 1 Muscle 2 Liver 3 Bones 4 Pancreas 5 Prostate 2 Cardiac enzymes are: 1 CPK 2 LDH 3 AsAT 4 Amylase 5 Alkaline phosphatase 3 Which from indicated enzymes in blood serum are used as diagnostic tools? 1 Amylase 2 Pepsine 3 Rennine 4 Creatine phosphokinase 5 Catalase 4 Normal urine does not contain the substance: 1 Urea 2 Creatinine 3 Creatine 4 Uric acid Ammonium 5 salts 5 Which enzymes are used as drugs? 1 Pepsine 2 Trypsine 3 Chymotrypsine 4 Collagenase 5 Asparaginase 6 The lactate dehydrogenase (LDH) levels in blood serum are increased in: 1 Myocardial infarction 2 Acute pancreatitis 3 Diabetes mellitus 4 Acute glomerulonephritis 5 All of above 7 The main pathway for ATP synthesis from ADP in liver is: 1 Reaction with GTP 2 Oxidative phosphorylation 8 9 10 11 12 13 14 3 Substrate phosphorylation 4 Reaction with Pi 5 Reaction with CTP The precursors for UMP synthesis are: 1 Carbamoylphosphate and Aspartate 2 Nicotinamide and Glutamate 3 Inosinic acid and Aspartate 4 Thymidine and Phosphate 5 Thymine and Ribose The pyrimidine nitrogen is excreted from the organism primarily in the form of: 1 Uric acid 2 Creatinine 3 Ammonium salts 4 Urea 5 Creatine δ-Aminolevulinic acid is synthesized from: 1 Succinyl-CoA and Glycine 2 Aspartate and Carbamoylphosphate 3 Aspartate and Glycine 4 Glutamate and Glycine 5 Acetyl-CoA and Oxaloacetate The activated amino acids can links with: 1 Pseudouridylic loop of tRNA 2 mRNA codon 3 tRNA anticodon OH-group of 3'-adenosine of the end 4 tRNA nucleotide 5 Phosphate of 5'end nucleotide of tRNA The postsynthetic modification of proteins may include: 1 Phosphorylation 2 Hydroxylation 3 Limited proteolysis 4 Covalent binding with prostetic group Heme is a component of: 1 Amylase 2 Peroxidase 3 Pepsin 4 Myoglobin 5 Cytochromes The blood buffer system includes: 1 Bicarbonate 2 Phosphates 15 16 17 18 19 20 21 3 Proteins 4 Hemoglobin The sourse of NH2-group in the synthesis of AMP from inosinic acid is: 22 1 Urea 2 Aspartate 3 Asparagine 4 Carbamoylphosphate 5 Ammonium salts The direct substrates for DNA synthesis 23 are: Deoxyribose, phosphate and nucleic 1 bases 2 Phosphate and deoxynucleosides 3 Deoxynucleoside triphosphates 4 Deoxynucleoside diphosphates 24 5 Purine and pyrimidine bases The end product of TMP catabolism in human is: 1 Uric acid 2 β-Aminoisobutyric acid 3 Inosinic acid 4 Creatine 25 5 β-Alanine Adenine is a component of: 1 FAD 2 NAD+ 3 CoA 4 PLP 26 5 Biotin The Inosinic acid in the organism is the precursor for synthesis of: 1 AMP 2 GMP 3 UMP 4 CMP 27 5 All indicated substances UMP is a component of: 1 tRNA 2 mRNA 3 DNA 4 rRNA 28 5 Mitochondrial DNA The amino acid which is formed in protein molecule as a result of postsynthetic modification is: 1 β-Alanine 2 Glycine 3 5-Hydroxylysine 4 Glutamine 5 Proline The distinguish peculiarities of tRNA include the presence of: 1 Anticodon 2 Adenosine on the 3'-end 3 Tertiary structure (conformation) 4 Large amount of minor nitrogen bases The transcription of mRNA may be regulated by: 1 Adrenalin 2 Noradrenalin 3 Cortisol 4 Vasopressin The direct donor of methyl group in the TMP synthesis: 1 Methionine 2 Methylmethionine 3 S-Adenosylmethionine 4 N5, N10 - CH2 - THF 5 Choline In the course of myocardial infarction the positive enzyme tests in blood includes: 1 Elevation of AST and ALT activity 2 Increase of LDH1 and LDH2 3 Elevation of Creatine kinase activity Elevation of MB isoenzyme of creatine 4 kinase Which components of urine are not patological? 1 Proteins 2 Ketone bodies 3 Glucose 4 Sulphates 5 Bilirubin Orotate is a precursor for synthesis of: 1 Purine nucleotides 2 Pyrimidine nucleotides 3 Heme 4 Cholesterol 5 Ketone bodies The source of NH2-group in the synthesis of GMP from inosinic acid is: 1 Aspartate 2 Glutamine 3 Glutamate 4 Carbamoylphosphate 5 Urea 29 The elevated level of acid phosphatase activity in blood serum indicates on disease of: 1 Heart 2 Muscle 3 Liver 4 Pancreas 5 Prostate 30 The conversion of dUMP into dTMP requires the coenzyme: 1 Positively charged amino acids are: 1. Asparagine 2. Glutamine 3. Lysine 4. Glutamate 5. Histidine 2 Which bonds do not splited during denaturation of protein? 1. Disulphide 2. Hydrogen 3. Peptide 4. Ionic 5. Hydrophobic 3 Biuret reaction will be positive with following substances: 1. Simple proteins 2. Dipeptide 3. Tripeptide 4. Amino acid solution 5. Gelatine 4 Tertiary structure of proteins is stabilised bythe following bonds: 1. Ether 2. Hydrophobic 3. Hydrogen 4. Ionic 5. Disulphide 5 What amino acid is the most abundant in the collagen molecule? 1. Histidine 2. Glycine 3. Asparagine 4. Leucine 1 2 3 4 5 6 7 NAD+ FAD THF PLP THB 5. Glutamate Amilase belongs to the class of enzyme: 1. Oxidoreductases 2. Hydrolases 3. Lyases 4. Synthetases 5. Isomerases Which from presented substances is a nucleotide? 1. Adenine 2. Adenosine 3. Cytidine 4. Prion 5. Adenosine monophosphate 8 The substances which do not bond with active site of enzyme: 1. Substrate 2. Product 3. Coenzyme 4. Competitive inhibitor 5. Allosteric effector 9 The nucleic acids are distinguished from proteins by means of: 1. They are high molecular substances 2. They have complicated tertiary structure 3. They absorbe the light in ultraviolet region 4. They do not contain amino acid residues 10 Which substance does not belong to natural minor nucleotides? 1. Methylcytidine phosphate 2. Hydroxymethylcytidine phosphate 3. Dihydrouridine phosphate 4. Pseudouridine phosphate 5. Uridine phosphate 11 The vitamin with the highest daily requirements for man: 1. A 2. B2 3. C 4. D 5. E 4. 60-100 mg/dl 5. No one from indicated values 17 Insulin independent diabetes mellitus occurs due to: 1. Disturbances of glycolysis regulation 2. Elevated insulin secretion 3. Elevated glucagone secretion 4. Reduced insulin secretion 5. Disturbances of insulindependent uptake of glucose 18 Hyperglycemia is observed under: 1. Tumor diseases of adrenal cortex 2. Hyperfunction of thyroid gland 3. Kidney diseases 4. Diabetes mellitus 12 Coenzyme is linked with apoenzyme: 1. In allosteric centre 2. In active centre 19 The enzymes which catalyze the 3. By means of different chemical irreversible glycolytic reactions: bonds 1. Phosphoglycerate kinase 4. Always tightly 2. Enolase 3. Phosphofructokinase 13 The vitamins, which do not contain the 4. Lactate dehydrogenase heterocycles in their structure: 5. Hexokinase 1. Retinol 2. Pyridoxine 20 The primer product formed during 3. Cholecalciferol glycogen splitting in muscle: 4. Riboflavin 1. UDP-glucose 5. All indicated vitamins 2. Glucose-1-phosphate 3. Glucose-6-phosphate 14 The specificity of holoenzyme is 4. Fructose-6-phosphate determined by: 5. Glucose 1. Lipid prosthetic group 2. Carbohydrate prosthetic group 21 Allosteric enzyme which regulates the 3. Apoenzyme synthesis of fatty acids: 4. Coenzyme 1. Acetyl-CoA-carboxylase 5. All of the above 2. Thiolase 3. Phosphofructokinase 15 Which hormones act through G-proteins? 4. Lipase 1. Adrenaline 5. HMG-synthase 2. Noradrenaline 3. Triiodothyronine 22 Recirculation between liver and intestine 4. Hydroxycortisone is typical for: 5. Glucagone 1. Phospholipids 2. Monoglycerols 16 The normal glucose level in man blood: 3. Glycerol 1. 3-5 g/l 4. Lysophospholipids 2. 0.6-1.0 g/l 5. Bile acids 3. 3.3-5.5 mmol/l 23 Into lymphatic system of intestine are absorbed: 1. Chilomicrones 2. LDLP 3. HDLP 4. VLDLP 5. LDLP and VLDLP 24 Phospholipids: 1. Lecithins 2. Cardiolipins 3. Acylglycerols 4. Ceramide 25 Precursor for prostaglandins: 1. Palmitate 2. Arachinate 3. Arachidonate 4. Stearate 5. Oleate 26 27 28 29 30 The substances which are formed from tyrosine 1. γ-Aminobutirate 2. Adrenaline 3. Noradrenaline 4. Dopamine 5. Phenylalanine 31 The activated amino acids are linked with: 1. Pseudouridylic loop of tRNA 2. mRNA codon 3. tRNA anticodon 4. 3-OH-group of ribose in final adenosine of tRNA 5. Phosphate on 5’-end of tRNA 32 Heme is a component of: 1. Amylase 2. Peroxidase 3. Pepsin In detoxification of ammonia take part the 4. Myoglobin amino acids: 5. Cytochromes 1. Histidine 2. Aspartate 33 The end catabolic product of TMP in man: 3. Glycine 1. Uric acid 4. Glutamate 2. β-Aminoisobutyric acid 5. Tryptophan 3. Inosinic acid 4. Creatine In creatine synthesis take part: 5. β-Alanine 1. Arginine 2. Leucine 34 The distinguished peculiarities of tRNA 3. Methionine are the presence of: 4. Serine 1. Anticodon 5. Glycine 2. Adenosine at 3’-end 3. Large amounts of minor The Substances that do not participate in nitrogen bases transamination: 4. Only deoxyribonucleotides 1. Glutamine and Asparagine 2. Lysine and Threonine 35 -Aminolevulinate is the intermediate 3. Isoleucine and Aspartate during synthesis of: 4. Phenylalanine and Tyrosine 1. Purines 5. Alanine and Valine 2. Pyrimidines 3. Heme Scatol and indol are detoxificated in liver 4. Cholesterol by: 5. Ketone bodies 1. Glycine 2. Glutamate 36 Protein degradation in cells takes place in: 3. α-Ketoglutarate 1. Proteasomes 4. Uridine diphosphoglucuronic 2. Lysosomes acid 3. Peroxysomes 5. Proline 4. Nucleus 5. Ribosomes 37 Establish the correlation between: 1 2 3 4 5 Glyceraldehyde Pyruvate Starch Sacharase Maltose A B C D E Polysaccharide Disaccharide α-Keto acid Triose Enzyme 38 Oxaloacetate is: 1. α-Keto acid 2. Pyruvate decarboxylation product 3. Biogenic amine 4. CAC metabolite 39 Establish the correlation between: 1 2 3 4 5 Alanine Serine Lysine Aspartate Tyrosine A B C D E Nonpolar amino acid Polar uncharted amino acid Polar negatively charged amino acid Aromatic amino acid Polar positively charged 40 The substance what does not belong to the steroid hormones: 1. Progesterone 2. Cortisol 3. Aldosterone 4. Testosterone 5. Calcitonine 41 Establish the correlation between: 1 Pepsin 2 Ribosome 3 Cytochrome c 4 Casein 5 Immunoglobulin A B C D E Hemoprotein Nucleoprotein Phosphoprotein Glycoprotein Simple protein 42 Isoelectric point of protein means: 1. The freezing point of water 2. The pH value optimum for enzyme action 3. The temperature optimum for enzyme action 4. The pH value under which the common charge of protein molecule is zero 5. No one of indicated states 43 The substance what contains CH3- end is: 1. Oxaloacetate 2. Pyruvate 3. Acetyl-CoA 4. Malate 5. Citrate 44 Establish the correlation between: 1 Acetone A 2 Acetoacetate B 3 βHydroxybutyrat e 4 Pyruvate C 5 Oxaloacetate E D 45 Establish the correlation between: 1 Serine 2 Cysteine 3 Methionine 4 Glutamine 5 Histidine A B C D E Thiomethyl group Imidasole group Amide group Sulfhydryl group Hydroxyl group 46 Pantothenic acid is a component of: 1. HS-CoA 2. CoQ 3. NAD+ 4. NADPH(H+) 5. FAD 47 Cyclopentanoperhydrophenanthrene is a component of: 1. Ubiquinone 2. Tocoferols 3. Phylloquinone 4. Corticosteroids 5. Androgens 48 Name the following substance: H C HO H3C O CH2 O PO3H2 N 1. 2. 3. 4. 5. FMN TPP PLP FAD NAD 49 The metabolites of pentose phosphate pathway: 1. Pyruvate 2. Citrate 3. Glucose-6-phosphate 4. Ribulose-5- phosphate 5. Glucose-1-phosphate 50 Establish the correlation between: 1 2 3 4 Carbamoyl phosphate Glycine Dopamine Serotonine 5 α-Ketoglutarate A B C D E Adrenaline synthesis Creatine synthesis CAC Decarboxylation of 5-hydroxytryptophan Urea synthesis 51 Coenzyme of dehydrogenases may be: 1. NAD+ 2. FAD 3. Pyridoxine 4. Biotin 5. CoA 52 Accumulation of acetyl-CoA in mitochondria will: 1. Accelerate the oxidative decarboxylation of pyruvate 2. Activate the gluconeogenesis 3. Inhibit the oxidative decarboxylation of pyruvate 4. Inhibit the gluconeogenesis 53 Establish the correlation between: 1 Accelerate lypolysis 2 Inhibit lypolysis A B Catecholamines Prostaglandins 54 The regulatory enzyme NH3-dependent carbamoylphosphate synthetase catalyzes the reaction: 1. Which requires the spend of 1 molecule of ATP 2. Which requires the spend of 2 molecule of ATP 55 Establish the consequence of action among the participants of hormonal signal transduction: 1 A cAMP 2 B G-protein 3 C Adenylate cyclase 4 D Membrane receptor 5 E Hormon 56 In blood of patient the glucose level was find the 2.9mmol/l. What sort of reasons might be? 1. High consumption of glucose 2. Overdose of insuline 3. Stress 4. Starvation 57 The Trommer reaction allows to detect: 1. Glucose 2. Riboso-5-phosphate 3. Starch 4. Sucrose 5. Ribose 58 Find the correlation between X (figure) and Y (letter) in the following chemical reactions: Dihydroxy-acetone phosphate X 1,3- Bisphosphoglycerate 1 Glyceraldehyde A Triosophosphate isomerase 2 2-Phosphoglycerate B Phosphoglycerate kinase 3 3-Phosphoglycerate C 4 5 2,3-Bisphosphoglycerate Glyceraldehyde-3phosphate D E Glyceraldehyde phosphate dehydrogenase Aldolase Phosphoglyceromutase 59 Find the correlation between the processes and its graphical representation: 1 A. B. C. D. 2 3 Dependence between OD and substrate concentration Dependence between the rate of enzymatic reaction and temperature Kinetics of lipase action Sugar curve (normal) 60 Urea cycle was discovered: 1. L. Paster 2. H. Krebs 3. A.E. Braunstein 4. V.A. Engelhardt 5. A. Meister Answers Amino Acids and Simple Proteins 1. 2. 3. 4. 5. 6. 7. 4 1, 3, 4, 5 3, 5 1, 4 2, 4, 5 3 3 5 19. 20. 21. 22. 23. 24. 25. 1, 5 2, 3, 4, 5 5 2 3 5 1, 5 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 2 1, 3, 5 3 1, 2, 3, 5 2 1, 2, 4 1, 2,3, 5 2 1, 2, 3, 4 4 4 26. 27. 28. 29. 30. 1, 2, 3 1, 2, 4, 5 1, 3 3 3, 4 Conjugated Proteins, Nucleic Acids and Enzymes 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 2 2 4 1 1 1,4 3 5 4 4 5 1 2 1 5 3 3 4 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 4 1 2 3 2,5 4 3 3 5 2,3,4,5 3 3 Vitamins, Lipids and Hormones 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 1,2,3,4 3 1,2,3,4 2,4 3 3 2,3,4 1,2,4 1 1,3 2 1 1,4 2 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 3,4 4 2 2 1 2 2,3,5 1,3 1,2,4 2 1,5 3 15. 16. 17. 18. 3,4,5 1,3,4 5 1,2, 3 Chemistry and Metabolism of Carbohydrates 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 1 2 2,3,4 4 3 1,2,3,4 4 1 5 1 2 3,5 1 5 4 4 3 1, 3, 5 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 2 1,2,4 4 5 4 2 2 2,3,4 3,4,5 2,3 2,3,4 2 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 3 1,5 2 4 2 2 2,4,5 3 3 3 1 4 Lipid metabolism 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 2,4 1,3,4 2,5 1 5 2 2,5 2 3,4,5 5 2 1,2,5 5 1 2 1 1,3,4 1,2,3,4 Amino acid metabolism 1. 3 19. 4 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 1 1 2 3 3 2 3,5 3 1 2 3 3 4 2 1,2, 3,4 5 3 5 1 4 1 1 1,2,3,4 2 3 2 1 1,2,3,4 Synthesis of protein, DNA, RNA. Metabolism of Conjugated Proteins 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 2,3 1,2,3 1,4,5 3 1,2,3,4,5 1 2 1 4 1 4 1,2,3,4 2,4,5 1,2,3,4 2 3 2 1,2,3 1,2 1,2,4 3 1,2,3,4 3 4 1,2,3,4 4 2 2 5 3 Example for Examination Test 1 2 3 4 5 6 7 8 9 10 3,5 3 1,3,5 2,3,4,5 2 2 5 2,5 4 5 21 22 23 24 25 26 27 28 29 30 1 5 1 1,2 3 2,4 1,3,5 2 4 2,3,4 41 42 43 44 45 46 47 48 49 50 1E,2B,3A,4C,5D 4 2,3 1B,2C,3E,4A,5D 1E,2D,3A,4C,5B 1 4,5 3 3,4 1E,2B,3A,4D,5C 11 12 13 14 15 16 17 18 19 20 3 2,3 1,3 3 1,2,5 2,3,4 5 1,2,4 3,5 2 31 32 33 34 35 36 37 38 39 40 4 2,4,5 2 1,2,3 3 1,2 1D,2C,3A,4E,5B 1,4 1A,2B,3E,4C,5D 5 51 52 53 54 55 56 57 58 59 60 1,2 2,3 1A,2B 2 1E,2D,3B,4C,5A 2,4 1,2,5 5C 1D,2A,3B,4C 2 Creator of the programme _______________________ Kuznetsova O.M. Director of the programme ______________________ Chernov N. N.