203?1,5,0,0,1,0,0What compounds are structural units of simple proteins and what type of linkage connects these structural elementsA. Mononucleotides b-glycosidic B. Glucose esterC. Amino acids peptide D. Fatty acids etherE. Glycerol disulfide?2,5,0,1,1,0,1What groups of amino acids are present in proteins and what is characteristic for themA. Hydroxyamino acids concern to the D-series B. Thioaminoacids concern to the L-seriesC. Heterocyclic amino acids are alpha-amino acidsD. Diamine dicarboxylic amino acids are beta-amino acidsE. Diamine monocarboxylic amino acids have optical activity ?3,5,1,0,1,0,0For tryptophan the following statements are correct:A. Is a heterocyclic amino acidB. Is a homocyclic amino acidC. Contains the heterocycle of indole D. Contains the heterocycle of imidazole E. Has acid properties?4,5,1,0,0,1,1For methionine and threonine the following statements are correct:A. Their pI is in neutral zone of рНB. Have one asymmetric atom of carbon each C. Have in the structure identical functional groupsD. Are the derivatives of the butyric acidE. Are the essential amino acids?5,5,0,1,0,0,0The aminoacids arginine and lysine have the following common propertiesA. Contain the guanidine residue B. At physiological рН have a positive chargeC. Are derivatives of the capronic acidD. Have several asymmetric atoms of carbon eachE. Form peptide bond using both amine groups?6,5,1,1,0,1,0

The total charge of proteins depends on:A. Amino acids structureB. pH of the solutionC. beta-COOH and gamma-NH2 groups of the polypeptide chainD. COOH and NH2 groups of the amino acid radicalsE. Hydrophobic radicals?7,5,0,0,1,1,1What statements about protein denaturation are correct:A. Destruction of primary structure increase of the biological activityB. No changing in the protein activity increase of the hydrophilityC. Destruction of tertiary structure increase of the hydrophobity D. Destruction of quaternary structure decrease of the biological activityE. No changes in the primary structure changes in the form of molecules ?8,5,0,1,1,1,1As colloidal solutions the proteins have the following properties:A. Increased speed of diffusion B. Low osmotic pressureC. Insignificant speed of diffusion D. High viscosityE. Optical properties? 9,5,1,1,0,0,1Concerning the primary structure of proteins the following answers are correct:A. Represents a sequence of amino acidsB. Is determined geneticallyC. Is stabilized by weak and noncovalent bonds D. Is broken at denaturationE. Is broken at hydrolysis ?10,5,1,1,1,0The correct statements concerning the peptide bond:A. Each peptide bond forms 2 hydrogen bondsB. Exists in two resonant formsC. Atoms O and H are situated in trans-position with regard to the bond C-N D. The bonds of alpha-carbon atom forbid the free rotationE. The atoms of the peptide bond and 2 alpha-carbon atoms are situated in the same plane

?11,5,0,0,1,1,0Secondary structure of proteins (correct answers): A. Is stabilized by hydrophobic and ionic interactionsB. There is only alpha-spiral or only beta-structureC. Is a result of the interaction of nearly located radicals of amino acidsD. Is stabilized by hydrogen bondsE. The bonds are formed within the limits of one chain only?12,5,0,1,0, 1,1Secondary structure of proteins (correct answers): A. Appears at the interaction of the closely situated chains onlyB. Represents alpha-spiral and beta-structureC. Is stabilized by disulfide bonds between the methionine radicals D. Is stabilized by disulfide bonds between the cystein radicalsE. Appears at the interaction in limits of a single chain or between two closely situated chains ?13,5,1,0,1,0,1Tertiary structure - correct statementsA. Packing of the polypeptide chain is in three-dimensional spaceB. Is stabilized by covalent bondsC. Is determined by the sequence of amino acids, their form and polarityD. Does not cause biological activityE. Is broken at the denaturation ?14,5,1,1,0,0,0Quarterly structure:A. is the result of protomers interaction with the formation of the functional protein B. is the result of the interaction of the contact surfaces of domainsC. Is stabilized by covalent bondsD. Does not collapse at denaturation E. The protein molecule has mobility? 15,5,0,1,1,1,0The following proteins have the quarterly structure:A. MioglobinB. HemoglobinC. FibrinogenD. Lactatdehydrogenase LDH1E. Serum albumin?16,5,1,0,0,1,0The correct statements about enzymes

A. Are biological catalystsB. Are inorganic catalystsC. Exist only in an active formD. In organism exist also in an inactive form E. Catalyze only reactions of synthesis?17,5,1,0,1,0,1The correct statements about the chemical nature of enzymesA. The main components are amino acidsB. Enzymes are termostable compoundsC. In water form colloidal solutionsD. Enzymes are micromolecular compoundsE. Can be degraded by proteases ?18,5,1,1,0,0,1General properties of both enzymes and non-biological catalystsA. Don’t change the direction of reactionB. Don’t change the equilibrium of a reversible reactionC. Catalyze the reaction in soft conditionsD. Catalyze the reaction in both directionsE. Are not spent during reaction?19,6,0,1,1,1,0Enzymes differ from inorganic catalysts by thatA. Accelerate thermodynamic possible reactionsB. Have specificityC. Have much greater catalytic efficiencyD. Catalyze the reactions in soft conditionsE. Reduce energy of activation of chemical process?20,5,1,0,1,1,1The active centre of an enzyme represents:A. An unique complex three-dimensional structureB. A point in the tertiary structureC. Cofactor enters in the structure of the active centre D. The active centre consists from catalytic and contact sitesE. The substrate is connected in the active centre ? 21,5,1,1,0,1,0The correct statements about the mechanism of enzymes’ actionA. Reduce the energy of activation of the reactionB. An enzyme-substrate complex is formedC. Enzyme-substrate complex is a stable, rigid structureD. Enzyme-substrate complex is an unstable structureE. The formation of enzyme-substrate complex does not change physical properties of enzyme

?22,5,0,1,1,1,0The correct statements about the mechanism of enzymes’ actionA. Substrate isn’t changed in the enzyme-substrate complex B. Substrate is deformed in the enzyme-substrate complex C. The complementarily of the active centre is induce by the substrateD. Enzyme-substrate complex reduces the substrate’s entropy, promoting the achievement of a transitive stateE. Enzyme-substrate complex raises entropy, increasing the level of the ??23,5,0,0,1,1,1Specificity of enzymes - correct statementsA. Depends on coenzymeB. Depends both on protein and coenzymeC. Can be absolute – the enzyme catalyzes the transformation of only one substrateD. Can be relative – the enzyme catalyzes the transformation of several substrates with an identical chemical bondE. Depends on apoenzyme?24,5,1,0,0,0,1Allosteric centre - correct statementsA. Is separated spatially from the active centreB. Is a place of substrate bindingC. Is characteristic for all enzymesD. Is the place for binding the compounds that have structural similarity to the substrate E. Is a place of metabolites, ligands binding? 25,5,1,0,1,0,0Allosteric enzymes - correct statements:A. Consist of two or more protomersB. Can have only one active and one allosteric centre C. The allosteric centre can join both activator and inhibitorD. The modulators are joined by covalent bond to allosteric centresE. Reaction kinetics is identical for allosteric and usual enzyme?26,5,0,1,0,1,1The main nitrogenous bases of DNA are:A. 5-methylcytosineB. cytosineC. 2-methyladenineD. guanineE. thymine

?27,5,1,0,1,0,1The main nitrogenous bases of RNA are:A. adenineB. xantineC. guanineD. thymineE. uracil?28,5,0,1,1,1,0The structural components of DNA are:A. dihydroxiuracilB. deoxyriboseC. phosphoric acidD. thymineE. ribosilthymine?29,5,0,1,0,0,1The structural components of tRNA are:A. inosineB. pseudouridineC. thymineD. deoxyriboseE. adenine? 30,5,0,1,1,0,0The next chemical bonds there are in the nucleic acids:A. peptide bondB. 3’,5’-phosphodiesterC. N-glycosideD. disulphideE. ester?31,5,1,0,1,0,1According the secondary structure of DNA are correctly:A. it is the double helix B. the chains are combined by the phosphodiester bondsC. the nitrogenous bases protrude into the interior of the helixD. the chains don’t separate at high temperatureE. it hasn’t the anticodon sites?32,5,0,1,0,1,1For RNA is correct:A. the cellular RNA content is constantB. is a single-stranded ribonucleotideC. is composed of AMP, GMP, TMP, CMP

D. the RNA-chain is polarE. the nucleotides are combined by 3’,5’-phospho-diester bonds?33,5,1,0,0,1,0For mRNA is correct:A. it transfers the genetic information from nucleus to ribosomesB. is the double-chain polynucleotideC. the 5’-end contains the CCA sequenceD. it contains the methyl-containing basesE. it has the small molecular mass?34,5,1,1,0,0,1The typical characteristics of DNA biosynthesis:A. replication is semiconservative processB. is needed the presence of double-chain mDNAC. is not needed a primerD. are needed only the deoxyribonucleoside phosphatesE. nucleus is the place for DNA synthesis?35,5,0,1,1,1,0Transcription:A. simultaneously is working whole chromosomeB. is assimetricC. are working only certain DNA sitesD. the double-helix of DNA is templateE. template is the noncodogenic DNA chain (-)?36,5,0,1,1,1,0The common characteristics of DNA and RNA biosynthesis:A. using the deoxyribonucleoside triphosphatesB. using the ribonucleoside triphosphatesC. the motive power of elongation is pyrophosphate hydrolysisD. the synthesis of chains goes in 5’ to 3’ directionE. the conservation of DNA template?37,5,0,1,0,0,1The RNA processing is:A. the Okazaki fragments bindingB. the 7’-methylguanine combines with 5’-endC. the addition of CCA-sequenceD. the place for processing is cytosolE. the nucleus is place for processing?38,5,1,0,0,0,1Genetic cod:A. is the triplet

B. is the singletC. codons are read in 3’ to 5’ directionD. on mRNA the codons are divided by nonsense codonsE. cod is degenerate (redundant)?39,5,0,1,0,1,1According translation is correctly:

A. synthesis of polypeptide chain starts on the C-endB. synthesis of polypeptide chain starts on the N-endC. initiative amino acid for procaryotes is methionineD. donor of formyl is the N10-formyl-FH4 E. formation of formyl-tRNA is catalized by specific transformylase?

40,5,1,0,1,0,1During protein biosynthesis for elongation is characterized:

A. formathion of peptide bondsB. connection of fmet-tRNA on the P siteC. using the 2 GTP moleculesD. formation the peptide bond between amino group of the P center

and carboxilic group of the A centerE. ribosome’s moving on one codon of mRNA?41,5,0,1,0,0,1Regulation of the anabolic vital cell processes is dependent on:A. presence of inductive enzymesB. presence of repressory enzymesC. presence of the constitutive enzymesD. coordinative inductionE. coordinative repression?42,5,0,1,1,0,1Enzymic character for telomerases:A. enzyme has the small activity “in viro”B. the human enzyme has high activityC. process is dependent on the length primerD. the primers are smaller of the 10 nucleotides are usedE. when the primer is more of the 10 nucleotides the DNA can have

the thousands of nucleotides?43,5,1,0,1,1,0Induction and repression of enzymes:A. induction is determined the “de novo” synthesis of the enzymic

moleculesB. repression is analog of retroinhibitionC. repression and induction are based on the economic principle in

the cell

D. repression is the inhibition of enzyme synthesisE. induction doesn’t define the new synthesis of enzyme molecules?44,5,1,1,1,1,1Mechanisms of the organism growing old:A. production of anomalic chromosome is increasedB. chromosomes loss are predominatedC. takes place the gene extraction near telomeraseD. after extraction of this gene the growing old repressor is

inactivatedE. the telomer binding proteins (TBP) are included in process?

45,5,1,0,0,1,0The confirmations relatively thymidine are correct:A. it is the deoxyribonucleosideB. it has only the lactim formC. it contains two N1-glycoside bondsD. it has the N1-C’1-glycoside bondE. it has the molecular structure C9H11O5N2?46,5,1,0,0,1,0For the adenilic acid is correct:A. it is consisted of nitrogenous base, pentose and phosphateB. it is the deoxyribonucleotideC. it has the alfa-glycoside bond D. it is AMPE. it is cAMP?47,5,1,1,0,1,0For mRNA is correct:A. is the structure of the “clover leaf”B. an amino acid is composed with 3’-OH of adenine nucleotideC. an anticodon loop consists of 3 nucleotidesD. an anticodon loop consists of 7 nucleotidesE. it consists about 50-60% of all content of cell RNA?48,5,1,1,0,0,0The Okazaki fragments:A. these are the short DNA fragmentsB. are sintetised in 5’ to 3’ directionC. these are noninformative DNA sitesD. are sintetised in 3’ to 5’directionE. are formed during synthesis of the leader DNA chain?49,5,0,1,0,1,1Codon AUG:

A. is the codon for cysteinB. is the initiative codon for translationC. is the initiative codon for transcriptionD. is the codon for methyonineE. is the codon for formyl-methyonine?50, 5,1,0,0,1,1Choose of the protein biosynthesis inhibitor for the replication:

A. streptomycinB. erythromycinC. puromycinD. mitomycin CE. canamycin?

51,5,1,1,0,1,1The functions of metabolism are the following:A. To supply the cells with chemical energyB. Transformation of nutritious substances into building blocksC. Synthesis of specific biomolecules onlyD. Catabolism of specific biomoleculesE. Assembling of polysaccharides and others cell components?52,5,0,1,1,0,1The following statements are correct:A. Catabolism is a stage of degradation of only exogenous substances B. Catabolism is a stage of degradation of various substances up to more simplesC. Catabolic processes are accompanied by gain of free energyD. The energy is collected only as ATPE. The energy can be collected both in ATP and in NADPН?53,5,1,1,0,1,0The following statements are correct:A. Anabolism is a stage of synthesis of various organic compoundsB. Anabolism consumes free energy (ATP)C. Anabolism requires hydrogen atoms delivered by NADНD. Anabolism has 3 stagesE. For anabolism is characteristic a convergence of metabolic pathways?54,5,0,0,1,1,1The following statements are correct:A. Catabolic and anabolic pathways have the same directionB. The speed of catabolic and anabolic pathways is regulated by common enzymes C. Catabolic and anabolic pathways differ in localizationD. Catabolic and anabolic pathways have a common third stage

E. Reactions of catabolic and anabolic pathways should be regulated separately?55,5,0,1,1,0,1Cycle ATP:A. ATP – is the main form of chemical energy storage B. In all alive cells carries out identical functionsC. It is an universal and main carrier of energyD. ATP is present only in mitochondriaE. In some biosynthetic reactions are used CTP, GTP, UTP?56,5,0,0,1,1,1The regulation of cell metabolism:A. ADP and AMP serve as allosteric inhibitors B. ATP serves as an activator D. The speed of the metabolism depends on the cell needs for ATPE. The speed of the metabolism depends on the ratio NADPH/NADPF. Depends on hormones ?57,5,1,1,1,0,0What compounds are macroergic: A. ADPB. ATPC. Creatine phosphateD. Diacylglycerol phosphate E. Glucose-6-phosphate?58,5,1,1,0,0,1The regulation of pyruvat dehydrogenase complexIs carried out by retroinhibition Acetyl CoA and NADH serve as inhibitors C. NADH inhibits E2D. Acetyl CoA inhibits E3E. The allosteric inhibition is amplified by macromolecular fatty acids?59,5,1,0,1,0,0Krebs cycle:A. Is a general final pathway of substances’ oxidation in living cellsB. All compounds are included in the Krebs cycle through acetyl CoAC. In the Krebs cycle Н+ and СО2 are formed from acetyl CoAD. The Krebs cycle works in anaerobe conditionsE. Oxygen directly participates in the Krebs cycle ?60,5,1,0,0,0,0Properties of alpha-ketoglutarate dehydrogenase complex (a-CGDH complex)

A. Includes as coenzyme derivatives of vitamins B1, B2, PP; HSКoA, lipoic acidB. a-CGDH complex is regulated by both covalent modification and allosterically C. Has a completely different action in comparison with pyruvate dehydrogenase complexD. NADH and succinyl-CoA intensify the activity of the a-CGDH complexE. The activity of a-CGDH complex is reduced by the low level of cell energetical status ?61,5,1,0,1,1,0Oxidation of succinate (6th reaction of Krebs cycle):A. Succinate is oxidized up to fumarate by dehydrogenation B. The reaction is catalyzed by succinate dehydrogenaze NAD-dependentC. Succinate dehydrogenaze (SDH) is an integrated membrane proteinD. FAD is connected by a covalent bond with histidine in the active centre of SDHE. FADH2 dissociate from SDH and the electrons are transferred to Fe +++?62,5,0,1,0,0,1Krebs cycle:A. One turn of Krebs cycle is accompanied by formation of 3 molecules of CO2B. In one turn of Krebs cycle only one acetyl radical is included C. Oxygen participates directly in Krebs cycle D. Krebs cycle works only in anaerobe conditionsE. Krebs cycle provides regeneration of 1 mol of oxaloacetate?63,5,0,0,0,1,0The transformation of 1 mole of isocitrate to succinate in the Krebs cycle provides the synthesis of ATP:A. 10 moleculesB. 12 moleculesC. 8 moleculesD. 7 moleculesE. 9 molecules?64,5,0,1,1,1,0Pyruvate carboxylase reaction:A. The reaction takes place in cytosolB. It is an anaplerotic reactionC. The reaction takes place in mitochondria D. It is a reaction of gluconeogenesis from alanineE. Does not require ions Mg ++ or ATP

?65,5,1,0,0,1,1Biological oxidation – the essence of process:A. It is the totality of oxidative and reductive processes that take place in cellsB. Occurs by addition of oxygenC. The transfer of electrons is realized directly to oxygenD. The oxidation is carried out by dehydrogenationE. The Н atoms are transferred as protons and electrons?66,5,1,1,0,1,0,The correct statements about the acceptors of Н + (е -)A. The acceptors of Н + (е -) are coenzymes of dehydrogenasesB. The electrons are the main source of energy in ATP synthesisC. NADН serves as an acceptor of electrons in reactions of biosynthesis D. NADPН serves as a donor of electrons in reaction of biosynthesis E. FADH2 is a donor of electrons in biosynthesis ?67,5,1,1,0,0,1Oxidative phosphorylation:A. The transfer of electrons through respiratory chain is connected with the ATP synthesis B. delta G of two electrons is equal to 52,6 kcalC. delta G of two electrons is enough to synthesize 5 molecules of ATPD. delta G of two electrons is enough to synthesize 1 molecule of ATPE. The synthesis of one molecule of ATP requires a Eo = 0,224V? 68,5,1,1,1,0,1The final products of electron transfer are:A. The addition to О2 of 2 electrons forms H2O2B. The addition to О2 of 4 electrons forms 2 Н2ОC. The addition to О2 of 1 electron forms superoxid (:O2 -)D. The transfer of 2 electrons through the complex II can form 3 molecules of ATPE. The transfer of 2 electrons through the complex IV can form 1 molecules of ATP ?69,5,1,1,1,0,0Mechanisms of oxidative phosphorylation:A. The Н ions come back to mitochondria through special ion channelsB. The flow of protons is driving force, which promotes synthesis of ATPC. ATP-sintase consists of the factors F0 and F1 D. Both factors are components if inner mitochondrial membraneE. ATP-sintase consists of 9 units of 5 different kinds?70,5,1,1,1,0,1

The control of oxidative phosphorylation:A. The P/O ratio characterizes the oxidative phosphorylationB. P/O ratio represents the number of moles of inorganic phosphate, transformed in the organic form at the utilization of 1 atom of oxygen C. P/O for malate oxidation is equal to 3/1 D. P/O for succinate oxidation is equal to 4/1E. As uncouplers can serve hydrasones, isothiocyanates ?71,5,1,1,1,0,0Call of the carbohydrate functions:A. energeticB. are the main components of cell membranesC. geneticD. stabilize an oncotic pressureE. are emulgators?72,5,0,0,0,1,1In human organism there are next carbohydrates:A. starchB. celluloseC. amyloseD. glucoseE. glycogen?73,5,0,1,1,1,0Lactose is:A. carborydrate which has the reduce property and 2 molecules of

beta-galactoseB. there is in the mammalia milkC. is the disaccharide with reduce propertyD. both of it’s monosaccharides have the pyranose formE. is the repeated structural subunit of glycogen? 74,5,1,0,1,0, 1What of these confirmations according glucose are correct:A. may be in alpha- and beta-form of stereoisomersB. the glucofuranose form is stableC. glucuronic acid is the product of glucose oxidationD. doesn’t have the hiral carbon atomsE. is the aldohexose with the 4 hiral carbon atoms?75,5,1,0,1,0,0Deoxyribose:A. is the component of certain nucleotidesB. is the component of mRNAC. is the modificated aldopentose

D. can’t be in the in the furanose formE. has the NH-group in place of OH-group?76,5,0,1,1,0,0Call the homopolysaccharides:A. heparinB. starchC. glycogenD. chondroitin sulphateE. heparan sulphate?77, 5,0,1,0,1,1Call the heteropolysaccharides:A. amylopectinB. hyaluronic acidC. maltoseD. keratan sulphateE. heparin?78,5,1,0,1,1,1For glucose absorbtion is needed:A. Na+-ions for production complex with monosaccharidesB. the abundance of Ca++-ionesC. participation of Na+ ,K+ -ATP-aseD. a coupling of oxydative phosphorylation in enterocytesE. presence of ATP and corresponding transport mechanism?79,5,0,1,1,1,0Breakdown of glucose to two trioses is correct:A. the end reaction is production of two aldosesB. equilibrium goes to C=O productionC. during these reactions produce one aldose and one ketoseD. are used 2 molecules of ATP as the result of five reactions E. all reactions of this step are indirect?80,5,1,0,1,1,0Oxidation of glyceraldehyde-3-phosphate:A. is catalysed by corresponding dehydrogenaseB. reaction is unreversibleC. reaction is reversibleD. is produced the energyE. reaction goes into mitochondria?81,5,0,0,1,1,0The end products of glycolysis:A. pyruvate

B. glucoseC. 2 ATPD. 2 H2OE. 2 CO2?82,5,1,1,1,0,0According pentose-phosphate oxidation of glucose the confirmations are correct:A. glucose-6-phosphate + NADP+ 6-phosphogluconolacton + NADP +

H+ B. reaction is catalysed by NADP-dependent dehydrogenaseC. lactonase catalyses of the 6-phosphogluconate productionD. lactonase is oxidoreductaseE. 6-phosphogluconate + NADP+ ribose-5-phosphate + CO2 + NADP

+ H+

?83,5,1,1,1,0,0End productes of one glucose molecule oxidation:A. 38 ATPB. 44 H2OC. 6 CO2 D. 22 H2OE. 44 ATP?84,5,1,0,1,0,1Substrates for gluconeogenesis:A. glycerolB. acetyl-coAC. glutamateD. acetoacetateE. asparagine?85,5,1,1,1,0,0Hyperglycemia may be at: A. diabetes mellitusB. pathology of the cortex of medulla glandsC. using the beta-blockatorD. hypothyrosisE. Addison’s disease?86,5,1,1,0,1,0Confirmations for maltose are correct:A. it is the product of enzymic hydrolysis of starchB. it is the product of enzymic hydrolysis of glycogenC. it is the cellulose monomerD. it is composed of two alfa-glucose molecules

E. doesn’t have mutorotation property?87,5,1,0,0,1,0Galactose:A. is the lactose monomerB. is the main carbohydrate of bloodC. is the keto-pentoseD. is the epimer of glucoseE. is alfa-anomer in the structure of lactose?88,5,0,0,1,0,0Fructose:A. is redused to D-sorbitol onlyB. is the ketose with L-stereoformC. is the galactose isomerD. is the main carbohydrate of bloodE. is the main component of lactose?89,5,1,0,1,0,0Homopolysaccharides:A. are cellulose, starch and hitinB. maltose is the structural subunit of celluloseC. cellulose is polysaccharide of plant D. cellobiose has 2 molecules of alfa-glucoseE. cellobiose has alfa-glycoside bond?90,5,0,1,0,0,1Confirmations about glycogenolysis are correct:A. this is hydrolysis of glycogenB. phosphorolysis of glycogen is the main processC. alfa-1,6-glycoside bonds of glycogen are broken by orto-phosphateD. glycogen phosphorylase is needed onlyE. alfa-1,6-bonds are broken by hydrolytic enzyme?91,5,0,1,0,0,1According the glycogenesis are the next confirmations:A. in the cardiac muscle and nerve (brain) tissue it goes activelyB. more active in the liver and skeletal muscleC. during glycogenesis are participated the “a” and “b”

glycogensynthetases onlyD. glycogen synthesis is needed of enzymic complexE. the 3 of macroergic molecules are needed for glycogen synthesis?92,5,1,1,0,1,0For Girke disease are correct the next confirmations:A. deficiency of glucose-6-phosphatase is the reason of this pathology

B. lactate and pyruvate are increased in the bloodC. glycogen’s structure is anomalic D. takes place the disturbances of liver, kidney and intestineE. reserve of glycogen is minimum? 93,5,0,0,1,1,1Enzymes for regulation of glycolysis:A. triose-phosphate isomeraseB. phospho-glucose isomeraseC. hexokinaseD. phosphofructokinaseE. pyruvate kinase?94,5,0,0,1,1,1Glycolysis activator is:A. NADHB. ATPC. AdrenalinD. Fructose-1,6-biphosphateE. AMP, ADP?95,5,0,0,0,1,1Inhibitors for glycolysis:A. NADB. CitrateC. GlucoseD. ATP E. Lactate?96,5,0,1,0,1,0NADH functions:A. the main factor for catecholamines productionB. inhibitor of Fe2+ oxidation into erythrocytesC. hydrogen is used in the gluconeogenesD. is need for synthesis and secretion of HCl in the stomachE. donor of H+ for Respiratory Chain?97,5,1,0,1,0,1What component is common for production of glucose from alanine and lactate?A. pyruvateB. lactate dehydrogenaseC. Mg2+ -ionsD. alanine aminotransferaseE. pyruvate kinase?

98,5,1,0,0,0,1The main functions of lipids:A. transportB. cataliticC. contractionD. geneticE. energetic?99,5,0,1,1,0,0Lipids as the components of cell membrane are:A. trigliceridesB. cholesterolC. phosphodiglycerideD. phosphatidyl ethanolE. free fat acids?100,5,0,0,0,1,0Neutral lipids are esters of the next components:A. ethanolamine and amino acidsB. sphingosine and fat acidsC. ethylenglycol and fat acidsD. glycerol and fat acidsE. cholesterol and fat acids? 101,5,0,0,0,1,0Biological role of phosphatidyl choline and phosphatidyl ethanolamine:A. the main components of fat tissueB. substrates for cholesterol productionC. energetic roleD. the main components of cell membraneE. the main components of nerve cell membranes?102,5,0,0,1,0,0Components of phospholipids are next amino acids:A. methionineB. cysteineC. serineD. tyrosineE. alfa-alanine?103,5,0,0,0,0,1What is ceramide:A. triacylglycerolB. phospholipidC. plasmalogenD. sterid

E. sphingomyelin? 104,5,1,0,1,0,0,Galactose is the component of:A. cerebrosidesB. gangliosidesC. sulpholipidsD. acetalphosphotidesE. sterids?105,5,0,0,1,0,0Sites and enzymes of triglycerides hydrolysis (digestion):A. intestinal lipase, the small intestineB. gastric lipase, stomachC. pancreatic and intestinal lipases, the small intestineD. lipoproteinlipase, intestineE. phospholipase, the large intestine?106, 5,0,0,1,1,0Bile acids are products of conjugation with the next component:A. cholesterolB. serineC. taurineD. glycineE. bilirubin?107,5,0,0,1,0,0Glycerophospholipids are hydrolyzed by:A. pancreatic lipaseB. intestinal lipaseC. phospholipaseD. coupled (conjugates) bile acidsE. cholesterolesterase?108, 5,0,0,1,0,0Production of lysophosphatidyl choline and lysophosphatidyl ethanolamine are catalyzed by :A. lipase (intestinal, pancreatic)B. phospholipase A1 C. phosphjlipase A2 D. phospholipase CE. phospholipase D?109, 5,0,0,0,1,0Phospholipids may be modificated to phosphatidyc acid by action of:A. phosphjlipase A1

B. phospholipase A2 C. phospholipase CD. phospholipase DE. all these enzymes?110,5,0,0,0,1,0The common intermediate of the triglycerides and phospholipids synthesis:A. diacylglycerolB. triacylglycerolC. phosphoglycerinic acidD. phosphatidyc acidE. monoacylglycerol?111,5,0,0,0,1,0Chylomicrons are breakdown by action of:A. triglyceridlipaseB. diglyceridlipaseC. monoglyceridlipaseD. lipoproteinlipaseE. phospholipase?112,5,0,1,0,0,0Hormone-sensible enzyme and hormones for fat acids mobilization:A. digliceridlipase insulinB. triglyceridlipase glucagon, cateholaminesC. monoglyceridlipase cateholaminesD. triglyceridlipase steroid hormonesE. diglyceridlipase cateholamines, glucagon?113,5,0,0,1,0,0Triglyceridlipase is activated by adrenalin and glucagon via the second messenger:A. inosytol mechanismB. cTMPC. cAMPD. Ca2+ -ionsE. production of enzymes by genom activation?114,5,0,0,1,0,0The common intermediate of the carbohydrates and glycerol catabolism:A. glyceraldehyde-3-phosphateB. 3-phosphoglycerinic acidC. dihydroxyacetone phosphateD. 2-phosphoglycerinic acid

E. 1,3-diphosphoglycerinic acid?115,5,0,0,0,1,0Transport of fatty acids from cytosol into mitochondria takes place in the form:A. free fat acidB. acyl-coAC. acyl-coQD. acylcarnetineE. acyl-coA and acylcarnetine?116,5,0,1,0,0,0How many number of acetyl-coA and cycles are the rezult of beta-oxidation of the fat acid with number of carbon atoms of 14?A. 7 and7B. 7 and 6C. 6 and 7D. 6 and 6E. 7 and 5?117,5,0,0,0,1,0The cetone bodies are:A. acetone, beta-cetobutiric acid, valerianic acidB. acetoacetic acid, alfa-hydroxybutiric acid, acetonC. beta-hydroxybutiric acid, alfa-ketobutiric acid, acetonD. acetoacetic acid, beta-hydroxybutiric acid, acetonE. acetic acid, butiric acid, aceton?118, 5,0,0,0,1,0Aceton is prodused during the next process:A. beta-oxydation of fat acidsB. glycolysisC. glycerol catabolismD. decarboxilation of acetoacetic acidE. reduction of glyceraldehyde-3-phosphate?119,5,0,1,0,0,0What substance is the donor of methyl-group for phosphatidylcholine production?A. methionineB. S-adenosylmethionineC. S-adenosylhomocysteine and CH3 –radicalD. methilcobalamine E. tetrahydropholic acid?120,5,0,0,1,0,0

At diabetus mellitus takes place the change in the acid-base equilibrium of blood:A. metabolic alkalosisB. gaseous (respiratory) acidosisC. metabolic acidosisD. gaseous (respiratory) alkalosisE. mixed acidosis?121,5,0,0,0,1,0For phosphatidylcholine production is needed:A. ADPB. TTPC. GTPD. CTPE. UTP?122,5,0,0,1,0,0For synthesis of conjugated bile acids are needed:A. taurine and cholesterolB. cysteine and uronic acidsC. glycocol and cholic acidD. methionine and deoxycholic acidE. taurine and chenodeoxycholic acid?123,5,0,1,1,1,0Biological functions of proteins:A. coenzymicB. cataliticalC. plasticD. transportE. energetic?124,5,0,1,0,1,0The essential amino acids are:A. arginineB. tryptophanC. glutamic acidD. phenylalanineE. tyrosine?125,5,0,1,1,0,1HCl functions are:A. activation of trypsinogenB. activation of pepsinogenC. pH optimum for pepsin activityD. pH optimum for lipase activity

E. denaturation of food proteins?126,5,1,0,1,0,1Caracteristics of pepsin:A. secrets from the main mucosal cells of stomachB. secrets from additional mucosal cells of stomachC. is activated by action of HCl into stomach cavityD. pH optimum is 3,0-4,0E. pH optimum is 1,0-2,0?127,5,1,0,1,0,1Characteristics of trypsin:A. secrets in nonactiv trypsinogen formC. is an exopeptidaseD. enterokinase is activator for trypsinogenE. intestine is a site for trypsin secretionF. mechanism of trypsin activation is partial proteolysis?128,5,0,1,0,1,0Trypsin and enterokinase:A. trypsin hydrolyzes the peptide bonds between lys and arg at N-

positionB. trypsin hydrolyzes the peptide bonds between lys and arg at C-

positionC. pH optimum for trypsin is 7,2-7,8D. pH optimum for trypsin is 8,2-8,8E. active enterokinase is glycoprotein?129,5,0,1,0,1,0Chymotrypsin:A. secrets of the intestinal mucosal cellsB. secrets of the pancreatic glandC. is an exopeptidase D. is an endopeptidaseE. is an activator for trypsinogen?130,5,0,0,1,0,1Carboxypeptidases:A. secret in active formsB. are the endopeptidasesC. carboxypeptidase A is a Zn-containing enzymeD. are nucleoproteinsE. are metalloproteins?131,5,0,1,1,0,0Aminopeptidases:

A. are endopeptidasesB. are exopeptidasesC. break a N-end amino acidsD. have an absolute specific activityE. Mg2+ is activator of aminopeptidase?132,5,0,1,1,0,0Dipeptidases:A. are endopeptidasesB. are exopeptidasesC. hydrolyze the dipeptidesD. are elastasesE. secret of the mucosal cells of stomach?133,5,0,1,0,1,0Absorbtion of amino acids:A. absorbate by simple diffusionB. absorbate by active diffusionC. use the Ca+-ATP-aseD. use the Na+,K+-ATP-aseE. transport of amino acids is antiport for Na+-ions diffusion?134,5,0,1,1,0,0Absorbtion of amino acids:A. takes place into stomachB. takes place into small intestineC. is needed the Na+-ionsD. is needed the Ca2+ -ionsE. takes place into large intestine?135,5,1,0,0,1,0gamma-Glutamyl transferase:A. glutathione is the cofactor of enzymeB. cysteine is the cofactor of enzymeC. glutamic acid is the cofactor of enzymeD. uses the energy of glutathione bondsE. use the energy of ATP?136,5,1,0,1,0,0Putrefaction of amino acids:A. production of toxic substances into large intestineB. production of toxic substances into small intestineC. indole is product of amino acid putrefactionD. histamine is product of amino acid putrefactionE. hippuric acid is toxic product of amino acid putrefaction?

137,5,1,0,0,1,1Putrefaction of amino acids:A. cadaverine is toxic productB. indikan is toxic productC. indole is toxic product of tyrosine degradationD. indole is toxic product of tryptophan degradationE. phenol is product of tyrosine degradation?138,5,0,1,0,0,1Amino acids are used for productions:A. uric acidsB. ureaC. ATPD. ceton bodiesE. creatinine?139,5,0,1,0,1,0The main pathways of amino acids catabolism:A. isomerizationB. transaminationC. epimerizationD. deaminationE. transmethylation?140,5,1,0,0,1,0Types of amino acids deamination in human tissues:A. direct oxidative deaminationB. hydrolytical deaminationC. intramolecular deaminationD. indirect oxidative deaminationE. reduce deamination of glutamic acid?141,5,1,0,0,0,0Direct oxidative deamination is correct for:A. glutamic acidB. aspartic acidC. glycineD. serineE. alanine?142,5,0,0,1,0,1Indirect deamination is correct for:A. glutamic acidB. asparagineC. aspartic acidD. serotonin

E. alanine?143,5,0,1,0,1,1Transamination is correct for:A. tryptamineB. glutamic acidC. serotoninD. aspartic acidE. alanine?144,5,1,0,0,1,0Reaction: HOOC-CH2-CHNH2-COOH + HOOC-(CH2)-CO-COOH HOOC-CH2 –CO-COOH + HOOC-(CH2)2-CHNH2-COOH A. is the transaminationB. is the decarboxylationC. is the direct oxidative deaminationD. is the reaction of AsATE. is the reaction of AlAT?145,5,0,1,1,0,0Transamination of alanine is:A. the production of oxaloacetateB. the production of pyruvateC. the reaction catalyzed by AlATD. an indirect processE. synthesis of biogenic amine?146,5,0,1,1,0,0Decarboxylation of amino acids:A. is production of ketone bodiesB. is production of biogenic aminesC. coenzyme for this reaction is vitamin B6D. coenzyme for this reaction is vitamin B1E. is production of ammonia?147,5,1,0,1,0,0Decarboxilation of histidine:A. is production of histamineB. is production of GABAC. is needed of pyridoxal phosphate coenzymeD. is needed of NAD coenzymeE. is production of serotonin?148,5,0,1,1,0,0Decarboxylation of hydroxytryptophan:A. is production of histamine

B. is production of serotoninC. is synthesis of hydroxytryptamineD. is needed of NAD coenzymeE. is catalyzed by AlAT?149,5,1,0,0,1,0Amino acids as precursors (substrates) for catecholamines production:A. phenylalanineB. glutamic acidC. arginineD. tyrosineE. glycine?150,5,1,0,0,1,0Production of ammonia (NH3) in the cells:A. direct oxidative deaminationB. transamination of amino acidsC. decarboxylation of histidineD. indirect oxidative deamination of alanineE. reduce amination of glutamic acid?151,5,1,0,1,0,0Urea production:A. takes place in the hepatocytesB. takes place in the kidneyC. is ornitine cycleD. is needed of B1 vitaminE. is needed of arginine?152,5,1,0,1,0,0Final products of ammonia detoxication:A. ureaB. uric acidC. ammonia saltsD. carbomoylphosphateE. glutamine?153,5,1,0,0,1,0Methionine:A. is essential amino acidB. is nonessential amino acidC. is basic amino acidD. is donor of CH3 group E. is donor for disulphide (S-S) bonds in protein structure?154,5,0,1,1,0,0

Puryne nucleotide production:A. is needed of carbomoylphosphateB. is needed of glycineC. precursor is inosine acidD. precursor is adenosine phosphateE. synthesis of AMP is needed of B1 vitamin?155,5,1,0,0,1,1Pyrimidine nucleotide production:A. is needed of carbomoylphosphateB. is needed of inosine acidC. vitamine B6 is used as coenzymeD. aspartic acid is substrate for synthesis of UMPE. glutamine is donor of amino group for CMP?156,5,0,1,1,0,0Monoaminooxidase:A. is enzyme for biogenic amines productionB. is enzyme for biogenic amine inactivationC. is enzyme for histamine inactivationD. catalyzes production of serotoninE. is the TDP-depended enzyme?157,5,1,0,1,0,0Allopurinol:A. is the inhibitor for uric acid productionB. is the activator for uric acid productionC. is decreased the uric acid concentration in the bloodD. is increased the uric acid concentration in the bloodE. is the substrate for xantine oxidase?158,5,1,0,1,0,1Chemical structure of hormones:A. simple proteinsB. carbohydratesC. complex proteinsD. glucose derivativesE. steroids?159,5,0,1,0,1,1Mechanism of hormone action:A. gamma-peptidasedB. membrane C. localD. membrane intracellular or indirectE. cytosolic or direct

?160,5,1,0,0,1,0Mechanism of hormone action:A. centralB. is needed of NADC. localD. peripheralE. TDP-dependent ?161,5,0,1,0,0,0Membrane mechanism:A. is specific for glucagonB. is specific for insulinC. is needed of 2,3-cAMPD. is characterized for steroid hormonesE. is characterized for thyroxin?162,5,1,0,0,1,0Adenylate cyclase mechanism:A. 3,5-cAMP is product of adenylate cyclaseB. 2,3-cAMP is product of adenylate cyclaseC. 3,5-cGMP is product of adenylate cyclaseD. ATP is substrate for adenylate cyclaseE. ADP is substrate for adenylate cyclase?163,5,0,0,1,1,03,5-cAMP:A. is substrate of guanylate cyclaseB. is cyclic dinucleotideC. is cyclic mononucleotideD. is secondary messengerE. is primary mediator?164,5,0,1,0,1,03,5-cGMP:A. is substrate of adenylate cyclaseB. is substrate of guanylate cyclaseC. is product of ATPD. is product of GTPE. is primary mediator?165,5,1,1,0,1,0Secondary messengers:A. 3,5-cAMPB. 3,5-cGMPC. 2,3-cAMP

D. Ca2=-ionsE. Mg2=-ions?166,5,1,0,0,1,0Specificity of hormone:A. 3,5-cAMP is secondary messenger for glucagonB. glucagon is activator of gluconeogenesisC. hydrocortisone is activator of gluconeogenesisD. adrenalin is activator of glycogenolysisE. adrenalin is activator of glycogen production?167,5,0,1,1,0,1Adrenalin:A. is hypoglycemic hormoneB. is hyperglycemic hormoneC. 3,5-cAMP is second messenger for adrenalinD. 2,3-cAMP is second messenger for adrenalinE. has alfa- and beta-receptors on cell membrane?168,5,1,0,0,1,1Glucagon:A. is hyperglycemic hormoneB. is hypoglycemic hormoneC. 3,5-cGMP is second messenger for glucagonD. is activator of glycogenolysisE. alfa-cells of pancreatic gland secret glucagon?169,5,1,0,1,0,1Insulin:A. is simple proteinB. is complex proteinC. is hormone with membrane mechanism actionD. is hyperglycemic hormoneE. is hypoglycemic hormone?170,5,1,0,0,1,0Insulin:A. is anabolic hormoneB. is catabolic hormoneC. is amino acid derivativesD. is dimer in active formE. is trimer in active form?171,5,0,1,1,0,0Hypothalamic hormones:A. are complex proteins

B. are polypeptidesC. are liberins and statinsD. are somatotropinsE. corticotropins?172,5,1,0,1,0,1Hypophyseal hormones:A. somatotropinB. somatoliberinC. thyrotropinD. thyroliberinE. lutropin?173,5,1,0,0,1,0Vasopressin:A. is activator of water reabsorbtion in the distal tubes of kidneysB. is diuretic hormone (increase of diures)C. is activator of cGMP protein kinasesD. is activator of cAMP protein kinasesE. is antidiuretic hormone?174,5,0,1,0,1,0Somatotropin:A. is catabolic hormoneB. act via 3,5-cAMP second messengerC. act via 3,5-cGMP second messengerD. is growth hormoneE. is anabolic hormone?175,5,1,1,0,0,1Thyroidal hormones:A. are iodothyroninesB. thyroxine is tetraiodothyronineC. thyroxine is complex proteinD. thyroxine has membrane mechanism actionE. calcitonin is thyroidal hormone?176,5,1,1,0,1,0Calcitonin and parathyrin:A. are hormones of parathyroid glandsB. calcitonin is hormone of thyroid and parathyroid glandsC. calcitonin increases Ca2+-iones concentration in the bloodD. calcitonin decreases Ca2+-iones concentration in the bloodE. parathyrin decreases Ca2+-iones concentration in the blood?177,5,1,0,0,1,0

Pancreas hormones:A. insulin secrets from beta-cells of pancreasB. insulin secrets from alfa-cells of pancreasC. glucagon secrets from beta-cells of pancreasD. insulin is hypoglycemic hormoneE. glucagon is hypoglycemic hormone?178,5,1,1,0,0,1Adrenal cortex hormones:A. are steroid hormonesB. are corticosteroidsC. have membrane mechanism actionD. are derivatives of amino acidsE. cholesterol is substrate for production of aldosterone?179,5,0,0,1,0,1Aldosterone:A. is simple proteinB. is regulator of Ca2+-ions concentration in the bloodC. is mineralocorticoidD. is glucocorticoidE. is regulator of Na+ and K+ concentration in the blood?180,5,1,0,1,0,0Glucocorticoids:A. are steroid hormonesB. decrease glucose concentration in the bloodC. increase glucose concentration in the bloodD. have membrane mechanism of actionE. have cytosolic (direct) mechanism action?181,5,1,0,0,1,1Sex hormones:A. are steroid hormonesB. are catabolic hormonesC. have membrane-cytosolic mechanismD. estradiol and testosterone are sex hormonesE. have direct (cytosolic) mechanism of action?182,5,0,0,1,1,0Prostaglandins:A. are steroid hormonesB. have membrane-cytosolic mechanism action via 3,5-cAMPC. are hormone-like compounds (hormonoids)D. are compounds derived from C20-polyene fatty acidsE. are antihormonal action

?183,5,1,0,1,0,1Blood functions:A. transportB. catabolicC. bufferingD. cataliticalE. hemostatic?184,5,1,0,1,0,1Proteins of blood:A. albuminsB. prolaminsC. globulinsD. histonesE. lipoproteins?185,5,1,0,1,1,0Enzymes of blood:A. alanyl aminotransferase (AlAT)B. hitinaseC. lactate dehydrogenase (LDH)D. acetylcholine esteraseE. uricase?186,5,1,0,0,1,1Nonproteinic nitrogenous compounds:A. ureaB. cholesterolC. glucoseD. uric acid E. creatinine?187,5,0,1,1,0,0Carbohydrates of blood:A. maltoseB. glucoseC. fructoseD. lactoseE. glycogen?188,5,1,1,1,0,0Lipids of blood:A. cholesterolB. triacylglyceridesC. phospholipids

D. waxesE. acetone?189,5,1,1,0,0,1Mineral components of blood plasma:A. Na+ (sodium)B. K+ (potassium)C. acetoneD. glycerolE. Cl- (chlorid)?190,5,1,0,0,1,0Macroelements of blood plasma:A. NaB. MnC. CrD. KE. Se?191,5,1,0,0,1,1Buffer systems of blood:A. bicarbonateB. arsenateC. glutamateD. phosphateE. proteinic?192,5,1,0,0,1,1Metabolic acidosis:A. increases concentration of acids in the bloodB. increases concentration of urea in the bloodC. increase concentration of CO2 in the bloodD. is production of ketone bodiesE. takes place at diabetes mellitus?193,5,0,0,1,1,0Gaseous alkalosis:A. increases urea concentration in the blood B. increases concentration of Ca-iones in blood plasmaC. increases concentrations of Na and K-iones in bloodD. decreases concentration of CO2 in bloodE. increases concentration of Cl-iones in blood plasma?194,5,1,0,0,1,0Respyratory function of blood:A. hemoglobin is carrier of oxygen

B. gaptoglobin is carrier of oxygenC. oxyhemoglobin concentration in arteriolar blood is 67%D. oxyhemoglobin concentration in arteriolar blood is 97%E. carboxyhemoglobin is complex of hemoglobin and O2?195,5,1,0,0,1,0Hemoglobin forms:A. oxyhemoglobin is transport form of O2 in the bloodB. carboxyhemoglobin is transport form of CO2 in the bloodC. methemoglobin includes Fe2+ D. carbohemoglobin is transport form of CO2 E. oxyhemoglobin includes Fe3+

?196,5,0,0,1,1,0Carboanhydrase:A. is enzyme for production of anhydrasesB. is leukocytic enzyme onlyC. is enzyme for H2CO3 decompositionD. has high activity in the lungsE. is enzyme for production of carbohemoglobin?197,5,1,0,0,1,0Hemostatic function of blood:A. fibrinogen is blood plasma coagulating factorB. fibrinogen is thrombocytic coagulating factorC. vitamin K is blood plasma coagulating factorD. thrombinogen is nonactive factorE. thrombinogen is active factor?198,5,0,0,1,1,1Blood cloating factors:A. fibrinolysinB. heparinC. fibrinogenD. thrombinE. Hageman factor?199,5,1,1,0,0,1Natural anticoagulants:A. fibrinolysinB. antithrombinC. pelentanD. sincumarE. heparin?200,5,0,0,1,1,0

Synthetic anticoagulants:A. vikasolB. heparinC. pelentanD. dicumarinE. streptokinase?201,5,1,0,0,1,0Procoagulants:A. vitamin KB. vitamin B1 C. plasminD. vitamin D3 E. convertin?202,5,1,1,0,0,1Pathology of blood clotting:A. hemophiliaB. Christmas diseaseC. Edisson diseaseD. Hartnup diseaseE. Willebrand’s disease? 203,5,0,0,1,1,1Coagulating factors:A. plasminB. adrenalinC. fibrinogenD. Hageman factorE. trombin