Informatii colectie:

1. What compounds are structural units of simple proteins and what type of linkage
connects these structural elements?
2. The free carboxylic groups (COOH) are present in:
3. The free amino groups (NH2) are present in:
4. What compounds contain phosphorus?
5. What compounds contain nitrogen?
6. What functional groups are present in simple proteins?
7. What functional groups of proteins have acidic properties?
8. What functional groups of proteins have basic properties
9. What compounds contain SH-group?
10. What compounds contain OH-group?
11. Indicate biopolymers:
12. What groups of amino acids are present in proteins?
13. What constituent units of amino acids are present in polypeptide chain:
14. Indicate hydrophobic nonpolar amino acids:
15. Indicate hydrophylic polar amino acids:
16. Indicate basic amino acids:
17. Indicate acidic amino acids:
18. For histidine the following statements are correct:
19. For serine the following statements are correct:
20. For аrginine the following statements are correct:
21. For tryptophan the following statements are correct:
22. For lysine the following statements are correct:
23. For tyrosine the following statements are correct:
24. For methionine the following statements are correct:
25. The correct statements for glutamine are:
26. What amino acids solution has a higher positive charge at pH=6.0?
27. Isoelectric point of the tetrapeptide glu-asp-cys-ser is at the following pH:
28. What amino acids solution has a higher negative charge at pH=8,0?
29. Isoelectric point of the tetrapeptide arg-lys-his-ala is at the following pH:
30. The protein contains the following amino acids (in %): agr-10, lys-26, val-13, pro-35,
ala-8, gly-8. At the physiological pH the protein:
31. What tetrapeptide will move to anode at the physiologic pH?
32. For threonine the following statements are correct:
33. Amino acids arginine and lysine have the following common characteristics:
34. For aspartic acid the following statements are correct:
35. Summary charge of protein depends on:
36. Protein salting-out is:
37. What happen during the denaturation of protein molecule?
38. The following statements are correct for -alanine and -alanine:
39. The following compounds are used for identification of N-ending amino acid:
40. The following compounds are used for identification of C-ending amino acid:
41. The protein colloidal solutions have the following properties:
42. Stability of the protein in a solution is determined by:
43. Conditions for protein precipitation are:
44. Simple proteins have the following functions:
45. Primary structure of proteins:
46. The correct statements according to the primary structure of proteins:
47. Peptide bond has the following properties:
48. Which of the following statements are correct?
49. Secondary structure of protein:
50. According to secondary structure of protein the following statements are correct:
51. For -helix the following statements are correct:
52. For -structure are correct:
53. What amino acids can destabilize -helix?
54. According to the tertiary structure of proteins the statements are correct:
55. Tertiary structure of proteins:
56. Tertiary structure of proteins:
57. According to the tertiary structure of proteins the following statements are correct:
58. The quarternary structure of proteins:
59. The quarternary structure of proteins:
60. Indicate oligomers:
61. According to hemoglobin (Hb) the following statements are correct:
62. Peculiarities of collagen composition:
63. Collagen:
64. Collagen structure:
65. Peculiarities of tropocollagen:
66. For enzymes the following statements are correct:
67. Common feature of enzymes and nonenzymatic catalysts
68. Distinctions of enzymes from nonbiological catalysts are:
69. According to chemical natures of enzymes the following statements are corect:
70. According to enzymes the following statements are correct:
71. The correct statements about complex enzymes:
72. According to cofactors the following statements are correct:
73. According to cofactors the following statements are correct:
74. Indicate the correct statements according the intracellular organizations of enzymes:
75. Active center of enzyme is:
76. Active center of enzyme:
77. The following functional groups can be in the active center of enzymes:
78. According to the substrate the following statements are correct:
79. Allosteric center:
80. Allosteric enzymes:
81. According to enzyme mechanism of action the statements are correct:
82. The correct statements about enzyme mechanism of action are:
83. Mechanisms of enzyme activation are:
84. The common enzyme properties are:
85. Specificity of enzymes:
86. Thermolability of enzymes:
87. Influence of pH on the enzyme activity:
88. Carboanhydrase has the following type of substrate specificity:
89. What enzymes have stereochemical specificity?
90. The activation of the enzymes is possible by:
91. Specific inhibition of enzymes is possible by:
92. The characteristics of competitive inhibition (CI):
93. The correct statements about competitive inhibition are:
94. The following statements about competitive inhibitors (CI) are correct:
95. Noncompetitive inhibition characteristics are:
96. Characteristics of noncompetitive inhibition are:
97. The correct statements for allosteric inhibition are:
98. According to succinate dehydrogenase (SDH) and regulation of its activity the following
statements are correct:
99. According to pepsin and the mechanism of regulation of its activity the following
statements are correct:
100. Acoording to -amylase and regulation of its activity the following statements are
correct:
101. The mechanism of sulfanylamides action on enzymes is:
102. According to Km of enzymes the following statements are correct:
103. Katal is the amount of:
104. The specific activity of enzyme is the amount of:
105. International Unite is the amount of:
106. Isoenzymes are:
107. The speed of enzymatic reaction:
108. According to LDH-isoenzymes the statements are correct:
109. According to LDH-isoenzymes the following statements are correct:
110. Creatine phosphokinase (CPK):
111. Vitamin B1:
112. Vitamin B2:
113. The statements about coenzymes - derivatives of vitamin B2 are correct:
114. According to coenzymes FAD and FMN the statements are correct:
115. NAD+ coenzyme:
116. NADP+ coenzyme:
117. Vitamin B6 and its coenzymes:
118. Coenzyme A and pantothenic acid:
119. Vitamin H (biotin):
120. Vitamin B12:
121. Folic acid:
122. Ascorbic acid:
123. Which coenzymes have sulfer in their structures?
124. What vitamins are transformed in coenzymes after phosphorilation?
125. Microelements as cofactors:
126. Assembling of proteins:
127. Shaperonins:
128. Active peptides (endothelins):
129. Endothelins are synthesized:
130. For enzyme classification the statements are correct:
131. Oxidoreductases: 132. Oxidoreductases are:
133. Transferases:
134. Transferases are:
135. Hydrolases:
136. Hydrolases are:
137. Lyases:
138. Lyases are:
139. Isomerases:
140. Isomerases are:
141. Ligases:
142. Ligases are:
143. Major nitrogenous bases in DNA are:
144. Major nitrogenous bases in DNA are:
145. Select minor nitrogenous bases of nucleic acids:
146. Structural components of DNA are:
147. Structural components of DNA are:
148. Select types of chemical bonds that are not present in nucleic acids:
149. About DNA structure are true:
150. Select correct statements about adenosine:
151. Select correct statements about citidine:
152. Thymidine:
153. Uridine:
154. Deoxy-cytidine:
155. 5'-adenylic acid:
156. Properties of nucleic acid constituents:
157. Quantitative determination of nucleic acid at 260-280 nm is due:
158. Complete acid hydrolysis of nucleic acids:
159. The number of hydrogen bonds in double-stranded DNA sequence

160. Secondary structure of DNA:

161. Select correct statements about DNA:

162. Structural characteristics of DNA:
163. Select correct statements about DNA:
164. Select correct statements about DNA:
165. Select correct statements about DNA:
166. Select correct statements about DNA properties:
167. Select correct statements about nucleosome:
168. Select correct statements about nucleosome:
169. Select correct statements about nucleosome:
170. Histones:
171. Select correct statements about RNA:
172. Select correct statements about RNAm:
173. Select correct statements about RNAm:
174. Select correct statements about RNAt:
175. Select correct statements about RNAt:
176. Select correct statements about RNAt:
177. Select correct statements about RNAr:
178. Structure and function of ribosomes:
179. Replication is:
180. DNA biosynthesis requires:
181. Select correct statements about replication:
182. Select correct statements about replication:
183. The complex DNA-replicase includes:
184. The complex DNA-replicase includes:
185. Okazaki fragments:
186. Okazaki fragments:
187. DNA-polymerases (III):
188. DNA-polymerases (III):
189. DNA-polymerases (I):
190. RNA participates in replication:
191. Select correct statements about transcription:
192. Select correct statements about transcription:
193. Select correct statements about transcription:
194. Procariotic RNA polymerase:
195. Select correct statements about procariotic RNAp:
196. Common features of the DNA and RNA biosynthesis:
197. Select correct statements about eucariotic RNAp:
198. Select correct statements about activity of RNApol:
199. Termination of transcription is determined by:
200. Factor rho ( ρ ):
201. Select correct statements about polynucleotide phosphorylase:
202. The RNA processing is:
203. RNAm maturation in eukaryotes requires:
204. Select correct statements about RNAt maturation:
205. Biogenesis of RNAr includes the following:
206. RNA-dependent RNA-polymerase:
207. Select correct statements about RNA-dependent DNA-polymerase:
208. Select correct statements about DNA reparation:
209. Repair of thymine dimmer involves:
210. The process of DNA repairing involves:
211. Peculiarities of DNA replication in eukaryotes:
212. Select correct statements about genetic code:
213. Select correct statements about genetic code:
214. Select correct statements about genetic code:
215. AUG codon:
216. Molecular mutations can be made by:
217. Mutation by chemical modification of bases in a chain of DNA:
218. A transversion mutation is characterized by:
219. A mutation by deletion is characterized by:
220. Mutations in DNA that can not cause defects are:
221. Consequences of mutations:
222. Restriction enzymes:
223. Restriction enzymes:
224. Select correct statements about plasmids:
225. Plasmids:
226. Genetic engineering involves:
227. Genetic recombination, types:
228. Select correct statements about aminoacyl-tRNA-synthetases:
229. Activation of amino acids:
230. Aminoacyl - RNAt complex formation:
231. Aminoacyl - RNAt - synthetase:
232. Initiation of protein synthesis requires:
233. The initiation complex consists of:
234. Select correct statements about translation:
235. Elongation in protein biosynthesis requires:
236. Elongation step in protein biosynthesis is characterized by:
237. Termination of protein synthesis:
238. Select correct statements about termination of protein synthesis:
239. Posttranslational modifications are:
240. Posttranslational modifications are:
241. Processes using one molecule of GTP are:
242. Select the protein synthesis inhibitors:
243. Select inhibitors which block protein synthesis at the level of transcription:
244. Select inhibitors which block protein synthesis at the level of translation:
245. Regulation of protein biosynthesis is ensured by:
246. Regulation of anabolic pathways (gene expression):
247. Select correct statements about protein synthesis regulation:
248. Select correct statements about LAC-operon:
249. Select correct statements about LAC-operon:
250. Select correct statements about regulation of gene expression:
251. Enzymatic induction and repression:
252. About the shortening of DNA after replication:
253. Telomerase is:
254. Eukaryotic chromosome elongation:
255. Regulation of telomerase (TM) activity in somatic cells:
256. Select correct statements about telomeres and telomerase:
257. Body's aging mechanisms:
258. Metabolism
259. Functions of the metabolism are:
260. Following statements about metabolism are correct:
261. Metabolic pathways:
262. Catabolism:
263. Anabolism:
264. Catabolic and anabolic pathways:
265. Metabolism regulation:
266. Bioenergetics:
267. Free energy (ΔG):
268. ATP:
269. ATP hydrolysis types:
270. Energy produced during ATP hydrolysis is determined by:
271. ATP:
272. Energetic state of the cell:
273. During the hydrolysis of the following compounds are released more energy than during the
hydrolysis of one high-energetic bond to ATP:
274. During the hydrolysis of the following compounds are released more energy than during the
hydrolysis of one high-energetic bond to ATP:
275. The speed of the metabolic processes:
276. Which of the listed compounds are high-energetic:
277. Which of the listed compounds are high-energetic:
278. Polyenzymatic complex ‒ pyruvate dehydrogenase (PDH):
279. The pyruvate dehydrogenase complex (PDHc)
280. Role of the pyruvate dehydrogenase complex (PDHc):
281. Oxidative decarboxylation of pyruvate (first reaction):
282. Oxidative decarboxylation of pyruvate (reactions II and III):
283. Oxidative decarboxylation of pyruvate (final reactions - IV and V):
284. Regulation of the PDH complex activity:
285. Regulation of the PDH complex activity:
286. Regulation of the PDH complex activity:
287. The net reaction of pyruvate oxidative decarboxylation:
288. Select the vitamins that are components of the coenzymes from the pyruvate dehydrogenase
complex:
289. Select the vitamins that are components of the coenzymes from the
pyruvate dehydrogenase complex:
290. Select the coenzymes of the pyruvate dehydrogenase complex:
291. Select the coenzymes of the pyruvate dehydrogenase complex:
292. Krebs cycle:
293. Krebs cycle:
294. Reaction: Acetyl-CoA + oxaloacetate + H2O → citrate + HS-CoA
295. Citrate synthase:
296. Reaction: citrate ↔ isocitrate:
297. Reaction: Isocitrate + NAD+ ↔ alpha-ketoglutarate + CO2 + NADH + H+
298. Reaction: alpha-ketoglutarate + NAD+ + HS-CoA → succinil-CoA + CO2 +
NADH + H+
299. Alpha-ketoglutarate dehydrogenase complex:
300. Reaction: Succinyl-CoA + GDP + H3PO4 ↔ succinate + GTP + HS-CoA:
301. Reaction: succinate + FAD+ ↔ fumarate + FADH2:
302. Succinate dehydrogenase:
303. Reaction: fumarate + H2O ↔ L-malate:
304. Reaction: malate + NAD+ ↔ oxaloacetate + NADH + H+:
305. Select the regulatory enzymes of the Krebs cycle:
306. Select the substrate phosphorylation reaction from the Krebs cycle:
307. Krebs cycle regulation:
308. Select the vitamins that are needed for normal activity of Krebs cycle enzymes:
309. Select the vitamins that are needed for normal activity of Krebs cycle enzymes:
310. Select the coenzymes that are necessary for normal functioning of the Krebs cycle enzymes:
311. Select the coenzymes that are necessary for normal functioning of the Krebs cycle enzymes:
312. Anaplerotic reactions:
313. Reaction: pyruvate + CO2 + ATP → oxaloacetate + ADP + H3PO4:
314. Reaction: phosphoenolpyruvate + CO2 + GDP ↔ oxaloacetate + GTP:
315. Select the anaplerotic reactions:
316. Biological oxidation:
317. NAD+:
318. FAD:
319. Select NAD+-dependent dehydrogenases (DH):
320. Select NAD+-dependent dehydrogenases (DH):
321. Select FAD-dependent dehydrogenases (DH):
322. Respiratory chain (RCh):
323. The transfer of reducing equivalents through the respiratory chain (RCh):
324. Oxido-reduction systems of the respiratory chain:
325. Oxido-reduction potential (Eo) of the redox systems of the respiratory chain:
326. Oxido-reduction potential (Eo) of the redox systems of respiratory chain:
327. Consumption of the free energy (ΔG) of the respiratory chain:
328. Oxidative phosphorylation:
329. Respiratory chain complex I (NADH-CoQ reductase):
330. Respiratory chain complex II (succinate-CoQ reductase):
331. Respiratory chain complex III (CoQH2-cytochrome c reductase):
332. Respiratory chain complex IV (cytochrome oxidase):
333. Cytochromes:
334. The mechanism of oxidative phosphorylation:
335. The mechanism of oxidative phosphorylation:
336. ATP synthase:
337. ATP synthase:
338. Inhibition of respiratory chain (RCh):
339. Uncoupling agents:
340. Uncoupling agents:
341. Select the uncoupling agents:
342. Select the respiratory chain inhibitors:
343. Select the respiratory chain inhibitors:
344. Select the ATP synthase inhibitors:
345. Phosphorylation ratio (P/O):
346. The end products of the respiratory chain:
347. Uncoupling of oxidative phosphorylation:
348. Brown adipose tissue:
349. Select the processes that occur in the mitochondrial inner membrane:
350. Select the processes that occur in the mitochondrial matrix:
351. Glycerol-phosphate shuttle system:
352. Malate-aspartate shuttle system − select the cytosol reactions:
353. Malate-aspartate shuttle system − select reaction that occurs in the mitochondrial matrix:
354. The transport of reducing equivalents through the inner mitochondrial membrane:
355. Microsomal oxidation:
356. Microsomal oxidation:
357. Cytochrome P450:
358. Select the reaction catalyzed by catalase:
359. Select the reaction catalyzed by superoxide dismutase:
360. The functions of carbohydrates:
361. Select the carbohydrates that are present in the human body:
362. Monosaccharides are:
363. Relating to monosaccharides are true:
364. Relating to monosaccharides are true:
365. Monosaccharide belongs to D series if it is:
366. Relating to monosaccharides are true:
367. Reduction reactions of the monosaccharides:
368. Oxydation reactions of the monosaccharides:
369. Maltose:
370. Lactose:
371. Sucrose:
372. Glucose:
373. Galactose:
374. Fructose:
375. Deoxyribose:
376. Ribose:
377. Homopolysaccharides (homoglycans):
378. Select homoglycans:
379. Select heteroglycans:
380. Select the correct statements about carbohydrate:
381. Select the correct statements about carbohydrate:
382. Digestion of carbohydrates:
383. Lactose intolerance:
384. Glucose uptake:
385. Glycogen:
386. Glycogenolysis:
387. Glycogenolysis (reaction catalyzed by glycogen phosphorylase):
388. Glycogen phosphorylase:
389. Hormonal regulation of glycogenolysis:
390. Chemical reaction: Glucose-1-phosphate ↔ Glucose-6-phosphate:
391. Glucose-6-phosphate (Glc-6-P) obtained from glycogen in skeletal muscles:
392. Glucose-6-phosphate (Glc-6-P) obtained from glycogen in liver:
393. Breaking dawn of 1,6-glycosidic bonds of glycogen (glycogenolisis):
394. Select enzymes of glycogenolysis:
395. Glycogenogenesis:
396. Select enzymes of glycogenogenesis:
397. Glycogenogenesis (select correct reacions):
398. Glycogenogenesis (select correct statements about glycogen synthase):
399. Glycogen synthase:
400. Hormonal regulation of glycogenogenesis:
401. 1,6-glycosidic bond formation of glycogen (glycogenogenesis):
402. Glycogenin:
403. Use of glucose-6-phosphate (Glc-6-P) in the liver:
404. Glycogenosis (glycogen storage disease):
405. von Gierke's disease
406. Glucokinase:
407. Hexokinase:
408. Glycolysis:
409. Glycolysis:
410. Reaction: Glucose + ATP → glucose-6-phosphate + ADP:
411. Reaction: glucose-6-phosphate ↔ fructose-6-phosphate:
412. Reaction: fructose-6-phosphate + ATP → fructose-1,6-diphosphate + ADP:
413. Regulation of phosphofructokinase activity:
414. . Reaction: fructose-1,6-diphosphate ↔ glyceraldehyde-3- phosphate + dihydroxyacetone
phosphate
415. . Reaction: glyceraldehyde-3- phosphate ↔ dihydroxyacetone phosphate
416. Reaction: glyceraldehyde-3-phosphate + NAD+ + H3PO4 ↔ 1,3-bisphosphoglycerate +
NADH+H+
417. Reaction: 1,3- bisphosphoglycerate + ADP ↔ 3-phosphoglycerate + ATP
418. Reaction: 1,3- bisphosphoglycerate + ADP ↔ 3-phosphoglycerate + ATP
419. Reaction: 3-phosphoglycerate ↔ 2-phosphoglycerate
420. Reaction: 2-phosphoglycerate ↔ phosphoenolpyruvate + H2O
421. Reaction: phosphoenolpyruvate + ADP → pyruvate + ATP
422. Reaction: phosphoenolpyruvate + ADP → pyruvate + ATP
423. Reaction: Pyruvate + NADH+H+ ↔ lactate + NAD+
424. Ways to use pyruvate:
425. Anaerobic glycolysis reaction summary is:
426. The end products of anaerobic glycolysis are:
427. Select regulatory enzymes of glycolysis:
428. Glycolysis is activated by:
429. Glycolysis is inhibited by:
430. Alosteric activators (1) and inhibitors (2) of phosphofructokinase:
431. In glycolysis ATP is formed in reactions catalyzed by enzymes:
432. Select phosphorylation reactions at the substrate level:
433. Regulation of glycolysis:
434. Hormonal regulation of glycolysis:
435. Enzymes common for glycolysis and alcoholic fermentation:
436. What enzyme does not participate in aerobic glucose cleavage?
437. The end products of complete oxidation of glucose:
438. How many ATP molecules are produced from complete oxidation of pyruvate?
439. How many ATP molecules are produced from complete oxidation of lactate?
440. Alcoholic fermentation:
441. Common enzymes of glycolysis and gluconeogenesis:
442. Gluconeogenesis:
443. Gluconeogenesis:
444. Select compounds that serve substrate for gluconeogenesis:
445. Select compounds that serve substrate for gluconeogenesis:
446. Reaction: Pyruvate + CO2 + ATP + H2O → oxaloacetate + ADP + H3PO4:
447. Pyruvate carboxylase:
448. Reaction: Oxaloacetate + GTP ↔ phosphoenolpyruvate + CO2 + GDP:
449. Phosphoenolpyruvate carboxykinase:
450. Gluconeogenesis from lactate requires the presence of the following enzymes:
451. Reaction: Fructose-1,6-diphosphte + H2O → fructose-6-phosphate + H3PO4:
452. Fructose-1,6-diphosphatase:
453. Reaction: Glucose-6-phosphate + H2O → glucose + H3PO4:
454. Glucose-6-phosphatase:
455. For the synthesis of one molecule of glucose are required:
456. Activators of gluconeogenesis are:
457. Hormonal regulation of gluconeogenesis:
458. Select the reactions that are required to include glycerol in gluconeogenesis:
459. Gluconeogenesis from glycerol requires enzyme:
460. Gluconeogenesis from alanine requires enzymes:
461. Gluconeogenesis from aspartic acid requires enzymes:
462. Pentose-phosphate pathway of glucose oxidation:
463. Functions of pentose-phosphate pathway:
464. Reaction: Glucose-6-phosphate + NADP+ → 6-phosphogluconolactone + NADPH+H+:
465. Select reactions from oxidative stage of pentose-phosphate pathway:
466. Initial substances of pentose-phosphate pathway are:
467. The end products of the oxidative phase of pentose-phosphate pathway are:
468. Deficiency of glucose-6-phosphate dehydrogenase (Glc-6-P DH):
469. Non-oxidative phase of pentose-phosphate pathway:
470. NADPH:
471. Fructose metabolism in the liver (select reactions):
472. Enzymes required for fructose metabolism in the liver:
473. Fructose metabolism in skeletal muscles (select reactions):
474. Enzymes required for fructose metabolism in skeletal muscle:
475. Essential fructozuria:
476. Fructose intolerance:
477. Metabolism of galactose (select reactions):
478. UDP-glucose can be used:
479. Enzymes necessary for galactose metabolism:
480. Galactosemia:
481. Galactose intolerance:
482. UDP-glucuronate:
483. Synthesis of glucuronic acid (select reactions):
484. Synthesis of lactose:
485. In interprandiale intervals, blood sugar is maintained by:
486. Hyperglycemia may be conditioned by:
487. Hyperglycemia may be conditioned by:
488. Hypoglycemia can be caused by:
489. Diseases accompanied by hyperglycemia are:
490. Effects of insulin on carbohydrate metabolism in the liver:
491. Insulin stimulates:
492. Insulin causes:
493. Effects of insulin on lipid metabolism:
494. Insulin efects:
495. Hormonal regulation of glycemia:
496. Regulation of insulin secretion:
497. Synthesis of insulin:
498. Effects of alcohol on metabolism:
499. 2,3-bisphosphoglycerate:
500. 2,3-bisphosphoglycerate shunt (select reactions):
501. Lipids are:

502. Functions of lipids:

503. Structural classification of lipids:

504. According their biological role the lipids are classified as:

505. According their physico-chemical properties lipid are classified as:

506. In human cells and tissues the following fatty acids predominate:

507. For the human body the following fatty acids are essential:

508. Which fatty acid has the lowest melting point?

509. Which fatty acid has the lowest melting point?

510. Acylglycerols :

511. Glycerophospholipids:

512. Lecithins and cephalins:

513. Phosphatidylcholine:
514. Phosphatidylethanolamine:

515. Phosphatidylcholine and phosphatidylethanolamine:

516. What compounds have acidic properties?

517. Phospholipases:

518. Cardiolypin:

519. Sphingomyelines contain:

520. Sphingosine:

521. Cerebrosides:

522. Gangliosides:

523. Gangliosides contain in the structure:

524. Glycolipids:

525. Which of the following compounds contains phosphorus

526. Cholesterol:

527. Bile acids:

528. Bile acids metabolism:

529. Lipid components of cell membranes are:

530. Function of biological membranes (1) and the structural component responsible for this
function (2):

531. Main properties of the membranes:

532. Biological membranes are stabilized by:

533. The proteins of biological membranes:

534. Carbohydrates of the biological membranes:

535. Lipids are essential components of the diet, because:

536. Dietary fat digestion in adults:

537. Complete break-down of the triacylglycerols in the gastrointestinal tract requires:

538. Lipolytic enzyme action in the gastrointestinal tract:

539. The mechanism of phospholipases activation in the gastrointestinal tract:

540. Hydrolysis of dietary fat leads to formation of:

541. The mechanism of absorption of the lipid components in the gastrointestinal tract:

542. According micelles the following statements are correct:

543. Indicate how the products of lipid digestion are absorbed:

544. The fate of lipid digestion products absorbed in the intestine:

545. Chylomicrons:

546. Catabolism of chylomicrons :

547. Primary hiperchylomicronemia (hyperlipoproteinaemia type I) is characterized by:

548. VLDL:

549. VLDL catabolism:

550. LDL:

551. Catabolism of LDL:

552. Primary hypercholesterolaemia (type II hiperlipoproteidemia) is characterized by:

553. HDL:

554. Lipoprotein lipase:

555. LCAT (lecithin-cholesterol acyltransferase):

556. Activation of fatty acids (FA) (in beta-oxidation of fatty acids):

557. Activation of fatty acids (FA) (in beta-oxidation of fatty acids):

558. Transport of fatty acids (FA) from mitochondria in the cytoplasm in beta-oxidation:

559. Structure (CH)3N+-CH2 -CHOH-CH2 -COO- is:

560. Beta-oxidation of fatty acids (FA):

561. Lynen spiral (beta-oxidation) involves a sequence of four reactions. Their correct order is:

562. Transformation of acyl-CoA (the first reaction of beta-oxidation of fatty acids):

563. The products of Acyl-CoA dehydrogenation (in first reactions to beta-oxidation of fatty acids)
are:

564. The second reaction of beta-oxidation of fatty acids:

565. The product of the second reaction of beta-oxidation of fatty acids:

566. The third reaction of beta-oxidation of fatty acids:

567. Name the products of the third reaction of beta-oxidation and the enzyme that catalyzes this
reaction:

568. Select the 4th -reaction of beta-oxidation and the enzyme that catalyzes this reaction:
569. In the result of one turn of beta-oxidation the fatty acid undergoes the following changes:

570. How many turns are necessary(1), how many molecules of acetyl-CoA (2) and how many
molecules of ATP (3) is formed during complete oxidation of palmitic acid (C16):

571. Use of acetyl-CoA:

572. Use of acetyl-CoA:

573. Oxidation of polyunsaturated fatty acid requires:

574. Oxidation of fatty acids with odd number of carbon atoms:

575. Ketone bodies are the following compounds:

576. According the compound CH3-CO-CH2-COOH the following statements are correct:

577. Beta-hydroxy-beta-methylglutaryl-CoA can be used for:

578. Use of ketone bodies in tissues

579. Beta-hydroxy-beta-methylglutaryl-CoA:

580. Correct statements about the ketone bodies:

581. Ketonemia:

582. Acetoacetate - correct statements:

583. Differences between oxidation and fatty acid biosynthesis:

584. Biosynthesis of fatty acid

585. Biosynthesis of fatty acid:

586. Indicate the initial compound in the synthesis of fatty acids (1) and its transport form from
mitochondria in cytosol (2):

587. Acetyl-CoA transport from mitochondria in cytosol (fatty acid biosynthesis)

588. Indicate enzymes that are involved in acetyl-CoA transport from mitochondria in cytosol (in
fatty acid biosynthesis)

589. Biosynthesis of malonyl-CoA (fatty acid synthesis):

590. Fatty acid synthase:

591. Activator (1) and inhibitor (2) of the acetyl-CoA carboxylase (the regulating enzyme in the
synthesis of fatty acids):

592. For malonyl-CoA synthesis is used CO2 with labeled C14. Malonyl-CoA is used in the synthesis
of palmitic acid. Which of the C atoms of palmitic acid will be labeled?

593. Which of the carbon atoms of palmitic acid will be labeled C14, if for its synthesis acetyl-CoA
with labeled C14 at methyl group was used:

594. . NADPH serves as a donor of reducing equivalent in fatty acid synthesis. It is generated in the
following process:

595. Reactions of the biosynthesis of fatty acids:

596. The reaction of synthesis of beta-ketoacyl-ACP (in biosynthesis of fatty acids):

597. Reaction of beta-ketoacyl-ACP reduction (in biosynthesis of fatty acids):

598. Enzyme (1) and reaction product (2) the transformation of beta-hydroxyacyl-ACP (actual
biosynthesis of fatty acids):

599. Enzyme (1) and products of transformation (2) of enoyl-ACP (biosynthesis of fatty acids):

600. The first cycle of biosynthesis of saturated fatty acids with even number of carbon atoms:

601. Synthesis of palmitic acid molecules requires:

602. Elongation of fatty acids (synthesis of fatty acid with more than C16 in the chain):

603. Synthesis of monounsaturated fatty acid:

604. Polyunsaturated fatty acids:

605. Biosynthesis of triacylglycerols:

606. Biosynthesis of triacylglycerols:

607. Glycerol-3-phosphate is formed:

608. During the triacylglycerols biosynthesis the phosphatidic acid:

609. Common intermediate in the synthesis of triglycerides and phosphatides:

610. The phosphatidic acid will be used for biosynthesis of triglycerides or glycerophospholipids
in dependence of :

611. Lipotropic factors are:

612. Nucleotides with specific role in lipid biosynthesis are:

613. Name the source of methyl group in the synthesis de novo of phosphatidylcholine:

614. Synthesis of glycerophospholipids:

615. De novo pathway of glycerophospholipids synthesis:

616. Phosphatidylethanolamine synthesis from phosphatidylserine (de novo pathway of

glycerophospholipids synthesis):

617. Phosphatidylcholinesynthesis from phosphatidylethanolamine (de novo pathway of

glycerophospholipids synthesis):

618. Salvage pathway of phosphatidylcholine synthesis

619. Salvage pathway of phosphatidylethanolamine synthesis:

620. Phosphatidylinositols:

621. The precursors of sphingosine are:

622. Sphingosine:

623. In the synthesis of the sphingomyeline the following compounds participate:

624. In the synthesis of the cerebrosides the following compounds participate:

625. Sulfatides:
626. Catabolism of gangliosides:

627. Tay Sachs disease:

628. Niemann-Pick disease:

629. In the synthesis of the gangliosides the following compounds participate:

630. Biosynthesis of cholesterol:

631. Rate-limiting reaction in cholesterol synthesis is:

632. Regulation of cholesterol biosynthesis:

633. Metabolism of LDL (low density lipoproteins):

634. Causes of blood cholesterol increasing:

635. Atherosclerosis:

636. Obesity:

637. Alcoholic hyperlipidemia:

638. Biochemical mechanisms of diabetic dyslipidemia:

639. After a meal abundant in carbohydrates the following takes place:

640. Fatty degeneration of the liver ("fatty liver"):

641. In starvation occurs:

642. Lipogenesis is stimulated by:

643. Precursor of eicosanoids:

644. Eicosanoids:

645. The following compounds refer to eicosanoids:

646. Biosynthesis of eicosanoids:

647. Cyclooxygenase:

648. Biosynthesis of eicosanoids:

649. Lipoxygenase:

650. Regulation of the biosynthesis of eicosanoids:

651. Eicosanoids (mechanism of action):

652. Eicosanoids (biological effects):

653. Superoxide anion:

654.
Glutathione peroxidase:

655. Liposoluble vitamins:

656. Vitamin A:

657. Vitamin E:

658. Vitamin K:

659. Vitamin D:

660. Metabolism of vitamin D

661. Calcitriol:
662. Biological functions of proteins:
663. Biological functions of proteins:
664. Biological value of proteins is determined by the essential amino acids:
665. Biological value of proteins is determined by the essential amino acids:
666. Select the semiessential amino acids:
667. Correct statements about the chemical compound:
 CH2 - CH - COOH

NH2
NH
668. Correct statements about the chemical compound:
HOOC-CH2-CH2-CH-COOH
|
NH2
669. Correct statements about the chemical compound:
HOOC-CH2-CH2-CH-COOH
|
NH2
670. HCl role in the digestion of proteins:
671. HCl role in the digestion of proteins:
672. Regulation of pancreatic and intestinal juices secretion:
673.
Pepsin properties:
674. Pepsin properties:
675. Pepsin:
676. Trypsin:
677. Trypsin:
678. Trypsin:
679. Enterokinase:
680. Chymotrypsin:
681. Chymotrypsin:
682. Carboxypeptidases:
683. . Aminopeptidase:
684. Protease functions:
685. Absorption of amino acids (AA):
686. Absorption of amino acids (AA):
687. Absorption of amino acids (AA):
688. Gamma-glutamyl cycle:
689. Gamma-glutamyl cycle:
690. Putrefaction of amino acids in the intestine:
691. The products of amino acids putrefaction in the intestine:
692. Neutralization of putrefaction products of amino acids:
693. The products of amino acids putrefaction:
694. Chemical compound:
695. Regulation of protein digestion in the stomach:
696. Tissular usage of amino acids (AA):
697. General pathways of amino acids degradation:
698. Types of amino acid deamination:
699. Amino acid deamination (DA):
700. Oxidative deamination (DA) of the amino acids:
701. Direct deamination (DA) of the amino acids:
702. Direct oxidative deamination of glutamic acid:
703. . Direct oxidative deamination of glutamic acid:
704. Glutamate dehydrogenase:
705. Amino acid transamination (TA):
706. Amino acid transaminases:
707. Mechanism of amino acids transamination reaction (TA):
708. Amino acid transaminases:
709. COOH-CH2-CHNH2-COOH + COOH-CH2-CH2-CO-COOH ↔
COOH-CH2-CO-COOH + COOH-CH2-CH2-CH NH2-COOH
710. CH3-CHNH2-COOH + COOH-CH2-CH2-CO-COOH ↔
CH3-CO-COOH + COOH-CH2-CH2-CHNH2-COOH
711. Indirect amino acid deamination (transdeamination):
712. Transreamination of amino acids:
713. Alanine transdeamination:
714. Alanine transdeamination. Select the reaction of the process (1) and enzyme (2) that catalyzes
the reaction:
715. Alanine biosynthesis (transreamination):
716. Alanine biosynthesis (transreamination). Select the reaction of the process (1) and enzyme (2)
that catalyzes the reaction:
717. Transdeamination of aspartic acid:
718. Transdeamination of aspartate. Select the reaction of the process (1) and enzyme (2) that
catalyzes the reaction:
719. Aspartate biosynthesis (transreamination):
720. Biosynthesis of aspartic acid (transreamination). Select the reaction of the process (1) and
enzyme (2) that catalyzes the reaction:
721. Alanine aminotransferase (ALT):
722. Aspartate aminotransferase (AST):
723. Decarboxilation of amino acids:
724. Amino acids decarboxilases (AA):
725. Chemical reaction:
726. Chemical reaction:
727. Chemical reaction:
728. Chemical reaction:
729. Chemical reaction:
730. Chemical reaction:
731. Chemical reaction:
R-CH2-NH2 + H2O + O2 → R-COH + NH3 + H2O2
732. Chemical reaction:
NH2 NH2
| |
HOOC - CH- (CH2)2 - COOH → CH2 - (CH2)2 - COOH + CO2
733. Vitamins necessary for mono- and diaminoxidases activity:
734. The precursor of catecholamines is:
735. The precursor of histamine is:
736. Serotonin is synthesized from:
737. The end products of simple protein catabolism:
738. Ammonia is obtained in the following processes:
739. Ammonia is obtained in the following processes:
740. Chemical reaction:
Glu + NH3 + ATP → Gln + ADP + H3PO4
741. Glucose-alanine cycle:
742. Enzymes and coenzymes of the glucose-alanine cycle:
743. Ureagenesis:
744. Ureagenesis:
745. Urea cycle enzymes:
746. Urea cycle enzymes:
747. Amino acids − intermediates of the ureogenetic cycle
748. How many ATP molecules are required for the synthesis of one urea molecule?
749. How many high-energy bonds are necessary for the synthesis of 200 molecules of urea?
750. How many CO2 molecules are required for the synthesis of 100 molecules of urea?
751. Urea cycle (first reaction):
752. Carbamoyl phosphate synthesis (first reaction of urea synthesis):
753. Select ornithine cycle reactions:
754. Select ornithine cycle reactions:
755. Renal excretion of ammonia:
756. Which amino acids can be synthesized from the intermediates of the Krebs cycle , with the
participation of transaminases?
757. Select the compounds that can generate ammonia by deamination:
758. NH3 is used for:
759. NH3 is used for synthesis of:
760. Select the amino acids that carry NH3 from tissues to the liver and kidney:
761. Direct sources of nitrogen for urea synthesis are:
762. Glutamate dehydrogenase is a:
763. The end products of NH3 detoxification:
764. The connection between Krebs cycle and urea cycle:
765. Blood non-proteic nitrogen includes:
766. Blood non-proteic nitrogen includes:
767. How many ATP molecules are generated during the aerobic oxidation of one alanine molecule
to CO2, H2O and NH3?
768. Glycine:
769. Glycine is involved in the synthesis of:
770. Glycine is involved in:
771. Glutathione:
772. Glutathione:
773. Serine (Ser):
774. Serine (Ser):
775. Cysteine (Cys):
776. Cysteine (Cys):
777. Methionine:
778. Methionine (Met):
779. S-adenosylmethionine (SAM):
780. S-adenosylmethionine (SAM) serves as methyl donor in the synthesis of:
781. Homocysteine:
782. Phenylalanine (Phe) and tyrosine (Tyr):
783. Phenylalanine (Phe) and tyrosine (Tyr) are precursors of:
784. Synthesis of tyrosine (Tyr) from phenylalanine (Phe):
785. Hereditary diseases caused by defects of the enzymes involved in the metabolism of
phenylalanine and tyrosine:
786. Phenylketonuria:
787. Alcaptonuria:
788. Albinism:
789. Tryptophan (Trp):
790. Histidine (His)
791. Glutamic acid (Glu):
792. Glutamic acid (Glu):
793. Glutamic acid (Glu):
794. Biosynthesis of glutamine (Gln):
795. Aspartic acid (Asp):
796. Biosynthesis of asparagine (Asn):
797. Aspartic acid (Asp) is involved in the synthesis of:
798. Aspartic acid (Asp) participates in the:
799. Amino acids catabolism:
800. Amino acids catabolism:
801. In the catabolism of amino acids are involved the following enzymes:
802. In the catabolism of amino acids are involved the following enzymes:
803. In the catabolism of amino acids are involved the following vitamins:
804. Vitamin (1), cofactor (2) and chemical reaction (3) catalyzed by the cofactor:
805. Folic acid:
806. Tetrahydrofolic acid (TFH):
807. Tetrahydrofolic acid (THF):
808. Tetrahydrofolic acid (THF):
809. Tetrahydrofolic acid (THF) is the acceptor and donor of the following groups:
810. Biotin participates in:
811. Protein and carbohydrate metabolisms connection:
812. Carbohydrate and lipid metabolisms connection:
813. Protein and lipid metabolisms connection:
814. Protein deficiency:
815. Protein deficiency is characterized by:
816. Digestion of nucleoproteins:
817. Select the chemical compounds that are involved in purine nucleotides synthesis:
818. Select the chemical compounds involved in purine nucleotide synthesis:
819. Phosphoribosyl-pyrophosphate synthesis (PRPP) - the first reaction of purine nucleotide
synthesis:
820. Phosphoribosylamine synthesis from phosphoribosyl pyrophosphate (PRPP) - the second
reaction of purine nucleotide synthesis:
821. Inosine monophosphate (IMP):
822. Synthesis of AMP from inosine monophosphate (IMP):
823. GMP synthesis from inosine monophosphate (IMP):
824. Regulation of the purine nucleotides synthesis:
825. Regulation of the purine nucleotides synthesis:
826. Salvage of purine bases:
827. Pyrimidine ring atoms sources:
828. Pyrimidine nucleotide synthesis (formation of carbamoyl phosphate ):
829. Pyrimidine nucleotide synthesis (formation of carbamoyl phosphate):
830. Pyrimidine nucleotide synthesis (select the reactions):
831. Pyrimidine nucleotide synthesis (select the reactions):
832. Biosynthesis of cytidylic nucleotides:
833. Formation of deoxyribonucleotides:
834. Biosynthesis of thymidylic nucleotides:
 835. Biosynthesis of nucleoside diphosphates (NDP) and nucleoside triphosphates (NTP) from
nucleoside monophosphate (NMP):
836. The final product of purine nucleotides catabolism:
837. Products of uracil and cytosine catabolism:
838. Products of thymine catabolism:
839. Purine nucleotide catabolism (uric acid biosynthesis):
840. Gout:
841. Select hereditary defects that caue gout:
842. Clinical manifestations of gout:
843. Allopurinol:
844. These proteins belong to the class of chromoproteins:
845. Hemoproteins:
846. Hemoglobin (Hb):
847. Hemoglobin is involved in:
848. Heme biosynthesis (select the necessary compounds):
849. Heme biosynthesis (first reaction):
850. Heme biosynthesis (second reaction):
851. Heme biosynthesis (conversion of heme into protoporphyrin IX):
852. Porphyria:
853. Catabolism of hemoglobin (Hb):
854. Catabolism of hemoglobin (Hb):
855. Catabolism of hemoglobin (Hb) (Hb transformation in biliverdin):
856. Catabolism of hemoglobin (Hb) (biliverdinei transformation in bilirubin):
857. Indirect bilirubin:
858. Indirect bilirubin:
859. Conjugation of bilirubin:
860. Intestinal stages of bilirubin metabolism:
861. Renal excretion of bile pigments:
862. Serum bilirubin:
863. Causes of jaundice:
864. . Causes of jaundice:
865. Neonatal jaundice:
866. Prehepatic jaundice:
867. Hepatic premicrosomial jaundice:
868. Premicrosomial hepatic jaundice (bile pigments changes):
869. Causes of microsomal hepatic jaundice:
870. Microsomal hepatic jaundice (bile pigment changes):
871. Postmicrosomal hepatic jaundice:
872. Postmicrosomial hepatic jaundice (bile pigment changes):
873. Posthepatic jaundice is caused by:
874. Posthepatic jaundice (bile pigment changes):
875. Blood transport of oxygen (O2):
876. Factors that increase the affinity of hemoglobin (Hb) for oxygen (O2):
877. Factors that decrease the affinity of hemoglobin (Hb) for oxygen (O2):
878. Oxyhemoglobin:
879. Blood transport of carbon dioxide (CO2):
880. Carbhemoglobin:
881. Pathological forms of hemoglobin are:
882. Pathological forms of hemoglobin:
 883. The exchange of O2 and CO2 (select the reactions that occur in the lungs):
884. The exchange of O2 and CO2 (select reactions that occur in the tissues):
885. Hypoxia:
886. Sickle cell disease (HbS)
887. Hormones are:
888. Possess biological activity:
889. General properties of hormones:
890. Fundamental action of hormones:
891. Classification of hormones:
892. It is correct that:
893. Blood hormone level is adjusted by:
894. The specificity of hormone action is determined by:
895. Transformation in an active hormone is carried out by:
896. The hormone receptors are:
897. Hormone receptors properties:
898. Mechanism of hormones action:
899. Membrane-intracellular mechanism:
900. Membrane-intracellular mechanism:
901. Proteins "G":
902. Gs and Gi proteins:
903. Proteins "Gq"
904. Hormonal second messengers are:
905. Membrane-intracellular mechanism of action of cAMP-mediated hormones:
906. Adenylate cyclase:
907. Adenylate cyclase:
908. Cyclic nucleotides (cAMP, cGMP):
909. Cyclic AMP is
910. Phosphodiesterase:
911. cAMP and protein kinases:
912. Protein kinase:
913. NO-metabolic regulator:
914. After the hormonal effect occurs:
915. Phosphodiesterase:
916. Intracellular calcium signaling system:
917. The complex Ca2+-calmodulin regulates:
918. Calmodulin (CM):
919. Membrane-intracellular mechanism of hormones action mediated by diacylglycerol (DAG) and
inositol triphosphate (IP3):
920. Membrane-intracellular mechanism of hormones action mediated by diacylglycerol (DAG) and
inositol triphosphate:
921. Phospholipase C:
922. Cytosol-nuclear mechanism of hormones action:
923. Hypothalamic hormones:
924. Hypothalamic hormones:
925. Name the liberins:
926. Name the statins:
927. Hormones of adenohypophysis:
928. Name the hormones of adenohypophysis:
929. Hormones of adenohypophysis:
930. Hormones - derivatives of proopiomelanocortin (POMC) are:
931. Adrenocorticotropin (ACTH, corticotropin):
932. Adrenocorticotropin (ACTH, corticotropin):
933. Somatomamotropic hormones are:
934. Somatotropin (growth hormone) is:
935. Somatotropin effects:
936. Somatotropin:
937. Somatotropin:
938. Somatotropin:
939. Prolactin:
940. Prolactin:
941. Pituitary glycoprotein hormones are:
942. Thyrotropin (TSH) is:
943. Thyrotropin (TSH):
944. Gonadotropins:
945. Luteinizing hormone (LH):
946. -lipotropin: 
947. Hormones of neurohypophysis:
948. Vasopressin and oxytocin:
949. Vasopressin:
950. Vasopressin:
951. Oxytocin:
952. Thyroid hormones:
953. Iodothyronins :
954. Thyroid hormone synthesis involves the following steps:
955. Thyroglobulin:
956. Thyroglobulin:
957. Supply of iodine
958. Biosynthesis of thyroid hormones - iodine oxidation:
959. Biosynthesis of thyroid hormones - ioduration of tyrosine residues:
960. Biosynthesis of thyroid hormones - T3 and T4 release from thyroglobulin:
961. Transport of thyroid hormone is made by:
962. Thyroid hormones metabolism:
963. Regulation of thyroid hormones synthesis and secretion:
964. Mechanism of T3 and T4 action:
965. The metabolic effects of T3 and T4 :
966. The metabolic effects of T3 and T4 :
967. Hyperfunction of thyroid gland is manifested by:
968. Thyroid hypofunction is manifested by:
969. Thyroid hypofunction is manifested by:
970. Extracellular calcium homeostasis is provided by:
971. Parathyroid hormone:
972. Parathyroid hormone:
973. Effects of parathyroid hormone (PTH) on bone tissue:
974. Effects of parathyroid hormone (PTH) on renal tissue:
975. Effects of parathyroid hormone on the intestine:
976. Metabolic features of hypoparathyroidism:
977. Metabolic features of hyperparathyroidism:
978. Calcitonin is:
979. Regulation of the calcitonin secretion:
980. The metabolic effects of calcitonin:
981. 1,25 dihydroxy-cholecalciferol (calcitriol):
982. 1,25-dihydroxy-D3 (calcitriol): the control of synthesis and physiological action:
983. Pancreatic hormones:
984. Insulin:
985. Insulin:
986. Insulin - regulation of secretion:
987. Insulin - metabolism:
988. Insulin - mechanism of action:
989. Insulin:
990. The effects of insulin on glucose metabolism:
991. Insulin increases:
992. Effects of insulin on carbohydrate metabolism:
993. Effects of insulin on lipid metabolism:
994. Effects of insulin on protein metabolism:
995. Diabetes mellitus is characterized by:
996. Glucagon:
997. Glucagon:
998. Glucagon - regulation of secretion:
999. Glucagon - actions:
1000. Glucagon - actions:
1001. Gastrointestinal hormones:
1002. Gastrointestinal hormones:
1003. Somatostatin:
1004. Catecholamines are:
1005. Catecholamines biosynthesis:
1006. Storage, secretion and catabolism of catecholamines:
1007. Catecholamines (mechanisms of action):
1008. Catecholamines (mechanisms of action):
1009. Effects of catecholamines:
1010. Effects of catecholamines:
1011. Pheochromocytoma:
1012. Adrenal cortex:
1013. Corticosteroids contain (structural features):
1014. Corticosteroids - biosynthesis:
1015. Corticosteroids - transport:
1016. Metabolism of steroids:
1017. 17-ketosteroids:
1018. Glucocorticoids - regulation of synthesis and secretion:
1019. Glucocorticoids - actions:
1020. Glucocorticoids - action on the protein metabolism:
1021. Glucocorticoids - actions on carbohydrate metabolism:
1022. Glucocorticoids - actions on lipid metabolism:
1023. Glucocorticoids - action on bone metabolism:
1024. Glucocorticoids - effects:
1025. Mineralocorticoid hormones:
1026. Regulation of aldosterone synthesis and secretion depends on:
1027. Regulation of aldosterone synthesis and secretion by the renin-angiotensin system
1028. Angiotensin II:
1029. The metabolic effects of mineralocorticoids:
1030. Mineralocorticoids activates the following processes in the kidney:
1031. The metabolic effects of mineralocorticoids:
1032. Excess of glucocorticoids causes:
1033. Cushing's syndrome is characterized by:
1034. Corticosteroid deficiency causes:
1035. Aldosteron hypersecretion is found in:
1036. Hyposecretion of corticosteroids is characterized by:
1037. Aldosteronism (Conn syndrome) is characterized by:
1038. Practical use of corticosteroids:
1039. Sex hormones:
1040. Sex hormones are:
1041. Sex hormones:
1042. Regulation of synthesis and secretion of sex hormones:
1043. Androgens:
1044. Androgens:
1045. Catabolism of androgens:
1046. Androgens - metabolic effects:
1047. Androgens - physiological effects:
1048. Ovarian hormones (estrogen and progesterone):
1049. Estrogens - catabolism:
1050. The metabolic effects of estrogens:
1051. Physiological effects of estrogens:
1052. Functions of blood:
1053. Functions of blood:
1054. The main organic components of blood:
1055. The main organic components of blood:
1056. Formed elements of the blood:
1057. Formed elements of the blood:
1058. Name the non-protein nitrogen compounds of the blood:
1059. Name the non-protein nitrogen compounds of the blood:
1060. Azotemia occurs in:
1061. Non-nitrogen organic compounds in the blood:
1062. Non-nitrogen organic compounds in the blood:
1063. Electrolyte composition of the blood:
1064. Electrolyte composition of the blood:
1065. Electrolyte composition of the blood:
1066. Hypokalaemia:
1067. Plasma calcium:
1068. Changes in plasma calcium:
1069. Iron:
1070. Iron:
1071. Plasma proteins:
1072. The role of plasma proteins:
1073. Serum albumins:
1074. Serum albumins:
1075. Serum albumins:
1076. Serum albumins:
1077. Plasma globulins:
1078. Alpha1-globulins are:
1079. Alpha2-globulin are:
1080. Beta-globulin are:
1081. Gamma-globulins are:
1082. Hyperproteinemia:
1083. Hypoproteinemia:
1084. To maintain physiological pH of blood are involved:
1085. Select only plasma buffer systems:
1086. Select only erythrocytes buffer systems:
1087. Select buffer systems prsent both in plasma and in erythrocytes:
1088. Buffering capacity of plasma proteins is determined by:
1089. Buffering capacity of hemoglobin is determined by:
1090. Ratio of the buffer system components at physiological pH (7.4):
1091. The mechanism of action of bicarbonate and phosphate buffer systems:
1092. Metabolic acidosis is caused by:
1093. Metabolic acidosis is present in:
1094. Respiratory acidosis is caused by:
1095. Respiratory acidosis is present in:
1096. Metabolic alkalosis is caused by:
1097. Respiratory alkalosis is caused by:
1098. Select plasma blood coagulation factor initiating intrinsic pathway:
1099. Select which blood coagulation factor initiates extrinsic pathway:
1100. Select factors involved in blood clotting via the intrinsic pathway only:
1101. Select factors involved in blood coagulation via the extrinsic pathway only:
1102. Select the factors involved in blood clotting via both the intrinsic and extrinsic
pathways:
1103. Select the factors involved in blood clotting via both the intrinsic and extrinsic
pathways:
1104. Select the factors involved in blood clotting via both the intrinsic and extrinsic
pathways:
1105. The role of vitamin K in blood clotting:
1106. Prothrombin:
1107. Thrombin:
1108. Fibrinogen:
1109. Conversion of fibrinogen to fibrin:
1110. Polymerization and stabilization of fibrin (clot formation):
1111. The following compounds are involved in blood clotting (additional to plasma
factors):
1112. The following compounds are involved in blood clotting (additional to plasma
factors):
1113. The following factors are involved in blood clotting:
1114. Select platelet coagulation factors:
1115. Select anticoagulant substances:
1116. Select anticoagulant substances:
1117. Heparin:
1118. Select the fibrinolytic system factors:
1119. Select the fibrinolytic system factors:
1120. Transformation of plasminogen into plasmin takes place under the action of:
1121. Fibrinolysin:
1122. Functional classification of serum enzymes:
1123. Select secretory liver enzymes:
1124. Select enzymes hepato specific indicators:
1125. Select enzymes hepato specific indicators:
1126. Select enzymes cardio specific indicators:
1127. Select enzymes cardio specific indicators:
1128. Select organo specific kidney enzymes:
1129. Select organo specific brain enzymes:
1130. Select organo specific skeletal muscle enzymes:
1131. Select organo specific bone tissue enzymes:
1132. Kinins of the blood:
1133. Kinins of the blood:
1134. Liver function is:
1135. The liver and carbohydrate metabolism:
1136. The liver and carbohydrate metabolism:
1137. The role of the liver in lipid metabolism:
1138. Liver and protein metabolism: