Lesson 2, Module 1
Lesson 2, Module 1
The tertiary structure of protein is formed mainly due to
disulfide bonds between side radicals of one amino acid, only.
Point out it:
A. Cys --------B. Met
C. Asp
D. Lys
E. His
Primary structure of proteins is formed due to one type of
bonds. Point out it:
A. Peptide bond -------------B. Disulfide bond
C. Ester bond
D. Hydrogen bond
E. Metal bond
Polypeptide chains of collagen include specific amino acids.
Name one of them:
A. Hydroxyproline ------------------B. Formyl-methyonine
C. Cysteine
D. -alanine
E. Ornithine
There are many important protein functions in the human
organism. Point out that of them, which isn't peculiar for
proteins:
A. Catalyst
B. Transfer of substances
C. Antibody
D. Structural component of a cell
E. Solvent -----------------The solubility of proteins in saline
solutions is determined by their native structure. Point out the
protein, which will swell only in saline solution:
A. Elastin
B. Albumin
C. Myoglobin
D. Immunoglobulin
E. Pepsin
The proteins are able to carry out the regulatory function. Find
out those proteins:
A. Aminopeptidase
B. Insulin --------------------C. Collagen
D. Hemoglobin
E. Immunoglobulin G
All proteins are divided into simple and conjugated ones. Find
out the simple proteins among these ones:
A. Albumin of egg
B. Histone
C. Globulin of egg
D. Protamine ----------------------E. All the proteins above
The molecule of simple protein insulin contains two polypeptide
chains. Specify the level of protein organization, at which the
insulin is able to act as hormone:
Quaternary
Tertiary Primary
Secondary
A conformation after limited proteolysis
Choose the factor that causes the sedimentation of protein in
solution without denaturation:
Ammonia sulfate ------------Toluene
Sulfuric acid
Nitric acid
Sodium hydroxide
Histones are related to basic proteins. That is because there is
high content of basic amino acid residues in their structure. Point
out these amino acids:
lanine, Glycine
Asparagine, Glutamine
Arginine, Lysine --------------------Leucine, Valine
Tryptophan, Tyrosine
The mixture of proteins can be separated by salting-out. Specify
the reagent formula that is used for this purpose:
HNO3NaCl ---------------H3PO4C2H5OH
C6H6Point out the type of bond allowing the formation of
alpha-helix structure:
Ester bond between side chain radicals
Hydrogen bonds between peptide fragments --------------Disulfide
bond between two cysteine radicals
Electrostatic interaction
Hydrogen bonds between side-chain radicals
Protein properties may be changed under the influence of some
factors. Find out them:
Strong alkaline medium
Organic solvent
The temperature of the environment
Strong acidic medium
All the factors placed above -------------------The polypeptide
chain gets the globular structure after the formation of various
bonds between the radicals of amino acid residues. Specify the
strongest bond in the globular structure:
Disulfide bond
Hydrogen bond
Donor-acceptor bond
Electrostatic interaction
Hydrophobic interaction
The isoelectric point (I.P.) of a protein depends upon the amino
acids composition of the protein. Choose the amino acid which high
content decreases the I.P. value of protein:
lanine
Aspartic acid Histidine
Leucine
Tryptophan
Proteins are obligatory components of human diet. Specify the
function of proteins in this case:
Nutritive
Transport
Regulatory
Structural
Catalytic
Different functional groups may be found in the structure of
L-amino acid residues of proteins. Identify the group that is able
to form ester bond:
CH3SH
CONH2OH --------------------NH2The isoelectric point of simple
protein equals 7.2. Propose the pH of buffer solution used for the
electrophoresis method to separate this protein from the mixture
with a condition to leave it on the start line of carrier:
pH=7.0
pH=7.6
pH=7.4
pH=5.0
pH=7.2
All are aromatic amino acids EXCEPT:
A. Phenylalanine
B. Tyrosine
C. Tryptophan
D. Lysine -----------------E. Positions A and D are
correctNinhydrin is a reagent to prove the presence of alpha-amino
group in the structure of amino acid due to change of its color
(violet color is observed). Choose the amino acid whose solution
changes the color of this reagent in other way it becomes
yellow:
A. L-methionine
B. L-tyrosine
C. L-serine
D. L-proline ------------------------E. L-alanine
The content of these amino acids in the composition of acidic
protein pepsin is too big in comparison with the content of others
amino acids in it. Name them:
Lysine and Arginine
Valine and Leucine -------------------Aspartic acid and Glutamic
acid Alanine and Glycine
Tyrosine and TryptophanThe yellow color sediment appearance
after the addition of strong nitric acid to albumin solution is due
to the presence of aromatic acid residues in protein composition.
Choose those one:
A. L-methionine
B. L-tyrosine -----------------------C. L-serine
D. L-proline
E. L-alanine
What amino acid high content presence in the composition of
polypeptide chain does not allow the formation of alpha-helical
structure as secondary level of organization?
Proline ---------------------Alanine
Glycine
Serine
Threonine
What type of amino acids mainly is represented as residues in
proteins of human body?
L-(-amino acids
D-(-amino acids
D-(-amino acids
L-(-amino acids -------------------D-(-imino acids
The structural proteins are involved in maintaining the shape of
a cell or in the formation of matrices in the body. Point out shape
of these proteins:
A. Globular
B. Fibrous -------------------C. Stretch of beads
D. Planar
E. All of above
Which of the following bonds are intact during denaturation of
proteins:A. Hydrophobic bonds
B. Hydrogen bonds
C. Peptide bonds -----------------D. Ionic bonds
E. All positions are correct
Alpha helix and Beta pleated sheet are examples of:
A. Primary structureB. Secondary structure
----------------------C. Tertiary structure
D. Quaternary structure
E. All positions are wrong
Biuret test is mainly done for:
Polysaccharides
Proteins -----------------------Lipids
DipeptidesAny of the above
Half saturation test using salting-out is done for:
Albumin
Globulin --------------------Fibrin
Prothrombin
Haemoglobin
What class of proteins Albumins and Globulins are related
to?
A. Simple proteins ----------------------B. Glycoproteins
C. Chromoproteins
D. Metalloproteins
E. Lipoproteins
What physical-chemical properties are observed for fibrous
protein only?
Solubility in water
Solubility in lipids
Amphoteric properties
Elasticity -------------------Denaturation and renaturation
Lesson 3 , Module 1
The conjugated protein necessarily contains special component as
a non-protein part. Choose the substance that can't carry out this
function:
Glucose
HNO3 ---------------------Fe 2+
Heme
Phosphate anion
Which method is better suited to separate a mixture of compounds
into its individual components and detects small amounts (microgram
or even picogram) of material:
Dialysis
Paper chromatography
Ultracentrifugation ----------------Salting out
Spectrophotometry Point out a possible cause of
hypoproteinemia:
Affected liver cells ----------------Multiple myeloma
Decreased permeability of the capillary wall
Overeating
Paraproteinemia
Point out a possible cause of hyperproteinemia
Increased permeability of the capillary wall
Infection (disturbed the macrophage system)-----Affected
gastrointestinal tract
Nephritic syndrome
Diabetes mellitus
Which method is appropriate for the determination of total
protein content in the blood serum:
Salting out
Foles test
Dialysis
Electrophoresis
Biuretic method -------------------Choose the conjugated protein
in possession of following characteristics: quaternary structure -
4 polypeptide chains; non-protein part 4 hemes; function oxygen
transport in the blood:
Low Density Lipoprotein
Albumin
Immunoglobulin
Hemoglobin -----------------Ceruloplasmin
What compound serves as non-protein part of glycoproteins:
Cu 2+Fe2+Galactose -----------------Heme
Phospholipid
Which group of proteins being phosphoproteins posses an activity
but being dephosphorylated has lost the activity:
Hormones
Transfer of lipids
Transfer of vitamins
Enzymes -------------------Carriers through membrane
The conjugated protein necessarily contains special component as
a non-protein part. Choose the substance that can't carry out this
function:
Glucose
Salt of Hg2+ -------------------------Thiamine pyrophosphate
ATP
AMP
When the following amino acids are separated by running them on
agarose gel, at pH 7 (electrophoresis method), which one of them
will be slowest to the anodic end
Glycine
Valine
Aspartic acid
Lysine ----------------------Glutamic acid
Choose, please, the blood serum index used for estimation of
hyperproteinemia state:
The total content of proteins ------------------The content of
albumins
The content of acute phase proteins
The amino acid concentration
The total activity of all the enzymes
Proteoglycans are conjugated proteins containing different
polypeptide chains of core protein and glucose aminoglycan moiety.
Choose the class of conjugated protein that is related to
proteoglycan:
Phosphoprotein
Nucleoprotein
Lipoprotein
Glycoprotein -----------------------Chromoprotein
It is in need to use the heme with iron ion for the active
centers of cytochrome oxidase (the key enzyme of tissue
respiration). Name the class of this conjugated protein:
Flavoproteins
Nucleoproteins
Lipoproteins
Glycoproteins
Chromoproteins -------------------There is the use of
electrophoresis for separation of proteins of blood plasma to prove
diagnosis of diseased persons. Name the property of proteins that
is the basis for the principle of electrophoresis method:
Optical activity
The big mass of the molecule
The ability of swelling
The high viscosity of the solution
The net charge of the molecule -----------------Albumins of
blood plasma are negative charged under the condition of
electrophoresis method duration. What electrode name have you to
choose for albumins movement in the electric field?
Catode
Anode ---------------Silk electrode
Calomel electrode
Carbon electrode
The enzyme preparation cytochrome C is used for the improvement
of tissue respiration in newborns at asphyxia state. Name the class
of this conjugated protein:
Flavoproteins
Nucleoproteins
Lipoproteins
Glycoproteins
Chromoproteins ----------------The diseased person with
diagnosis acute kidney insufficiency is in urological department of
hospital. Choose the method for cleaning of this person`s blood
from low-molecular compounds which can cause toxic effect in the
organism:
Salting-out
Electrophoresis
Dialysis ---------------------Hydrolysis
Affine chromotography
The hormone receptors are related to the class of conjugated
proteins. Name it:
Flavoproteins
Nucleoproteins ---------------Lipoproteins
Glycoproteins
Chromoproteins
The phosphorylation (the attraction of phosphate group to the
substrate) of polypeptide chain is often used for stimulation of
biological activity of a protein. Name the class of conjugated
protein formed due to phosphorylation:
Nucleoproteins
Lipoproteins
Phosphoproteins -------------------Chromoproteins
Glycoproteins
All the proteins are divided into simple and conjugated ones.
Find out the conjugated protein among these ones:
A. Egg albumin
B. Histone --------------C. Myoglobin
D. Protamine
E. Egg globulin
Name the location of deoxyribonucleoproteins in a cell, but not
in the nucleus:
A. Lisosome
B. Cytoplasma
C. Mitochondria ---------------D. Microsome
E. Endoplasmic reticulum
Flavoproteins are usually catalysts in a cell due to the
presence of special vitamin fragment in their structure. Name this
vitamin:
A. Nicotin amide
B. Folic acid
C. Panthothenic acid
D. Riboflavin ---------------E. Ascorbic acid
Ceruloplasmin (the protein of blood plasma) contains copper ion
and therefore has blue color. Name the class of this protein:
Metalloproteins -----------------Lipoproteins
Phosphoproteins
Chromoproteins
Glycoproteins
The electrophoresis method is used for the separation of blood
plasma proteins. Name the parameter of the protein molecule that is
in need to determine the pH of buffer solution for separation of
proteins in electrophoresis method:
Isoelectric point ------------------The mass of the molecule
The diameter of the molecule
The solubility in the water
The solubility in lipids
Ultracentrifugation is in need in biochemical investigations
for:
The study of three-dimensional structure of the molecule
The separation of mixture from lo-molecular compounds
-----------------The receiving of subcellular fractions of a
cell
The investigation of chemical composition of organic
compound
The determination of primary structure of proteins
Complex proteins do various functions. Find out the function of
hemoglobin in erythrocytes:
Regulatory function
Catalytic function
Nutrition function
Transport function ---------------Protection against viruses
Triacylglycerols (TG) are synthesized in the liver but are
stored in adipose tissue. Name the class of proteins promoted the
transport of TG from the liver to adipocytes:
Metalloproteins
Lipoproteins ---------------Phosphoproteins
Chromoproteins
Glycoproteins
Name the class of proteins used for the formation of ribosome
subunits:
Flavoproteins
Lipoproteins
Phosphoproteins Ribonucleoproteins
---------------Glycoproteins
Toxic affection of liver results in dysfunction of protein
synthesis. It is usually accompanied by the following kind of
dysproteinemia:
Absolute hypoproteinemia*
Relative hypoproteinemia
Absolute hyperproteinemia
Relative hyperproteinemia
Paraproteinemia
Lesson 4 Module 1
Conjugated enzymes contain cofactors in their structure. Point
out the location of vitamin derivative cofactor in the structure of
enzyme:
Active centre -----------Allosteric centre
Hydrophobic fragment of structure
Hydrophilic fragment of structure
Near the metal-ion-cofactor in the structure
Only one factor can influence on the charge of amino acid
radicals in the enzyme active centre. Name it:
Temperature
Pressure
pH medium --------------The presence of a competitive
inhibitor
The surplus of a reaction product
One of the important properties of enzymes is their specificity
of action. Check up a type of specificity for salivary amylase:
Absolute ----------------Absolute group
Absolute relative
Relative group
Stereochemical
Some terms are used for the description of non-protein part of
an enzyme. Point out the term for non-protein part that easily
dissociates from polypeptide chain:
Apoenzyme
Coenzyme --------------Prosthetic group
Cofactor
Metall ions
The change of the temperature of environment from 0C to 38C can
cause this effect:
The probability of enzyme-substrate complex formation is
increased
A denaturation of enzymes occurs
The enzyme molecular charge changes
The substrate molecular charge changes
Enzyme action specificity varies
There are some factors influencing enzyme activity. Point out
one of them resulting in complete loss of enzymatic activity:
Vitamin H
arbon dioxide
T = 100 C -------------------P =101325 Pa
Sodium chloride solution
There are some characteristic sites in the enzyme structure.
Choose the most important site for enzyme function:
Allosteric centre
Active centre -----------------Cofactor
Apoenzyme
Catalytic site
Point out the factor that can cause the damage of enzyme
function in a cell:
Temperature 37C
The presence of activator of enzyme
pH medium about 7.2
The presence of a product of enzymatic reaction
The surplus of protons in a cell ----------------Enzymes are the
catalysts of protein nature. Name the property of enzymes which is
not represented at the inorganic catalysts:
Ability to the denaturation -------------Wide specificity
Inert to chemical substrates
Big half-life
Ability to lowering the energy to activate the reaction
The oxidation of a substrate may be catalyzed by enzyme -
flavoprotein that contains FAD as prosthetic group. Name, please,
the vitamin used for this non-protein part of enzyme formation:
Ascorbic acid
Nicotinamide
Riboflavin -----------------Biotin
Adenosine triphosphate
The enzyme hexokinase can catalyze the conversion of glucose or
fructose in tissues. Find out the type of this enzyme
specificity:
Absolute
Absolute group
Absolute relative
Relative group
Stereochemical
The catalytic site of active center of enzyme is used for:
Conversion of a substrate in the reaction ------Binding with the
substrate
Binding with activator
Binding with inhibitor
Removal of a product of the reaction
There are different cofactors in the structure of conjugated
enzymes but only one is used for transfer of amine group from amino
acid to ketoacid. Name it:
Carboxybiotin
Pyridoxal phosphate
Thiamine pyrophosphate
FAD
NAD
Some terms are used for the description enzyme components. Point
out the term of a protein part of conjugated enzyme:
A. Apoenzyme --------------B. Coenzyme
C. Prosthetic group
D. Cofactor
E. Metall ions
Oxidoreductase can contain prosthetic group with vitamin B2.
Name it:
A. Retinal
B. Flavin adenine dinucleotide (FAD) -----------C. Nicotinamide
adenine dinucleotide (NAD)
D. Pyridoxal phosphate
E. Ascorbic acid
A substrate molecule is destructed upon enzyme action, and the
water is used for the products structure formation. Name the enzyme
class:
A. Oxidoreductase
B. Hydrolase --------------C. Lyase
D. Ligase
E. Isomerase
A qualitative composition of product molecule is completely
identical to substrate one, but the structure is different. Name
the enzyme class:
A. Oxidoreductase
B. Hydrolase
C. Lyase
D. Ligase
E. Isomerase ----------------ATP molecules may be used for
Transferases and Ligases function. Point out the signs of ATP use
for Ligases class:
A. ATP is used for a substrate dephosphorylation
B. ATP is used for a substrate phosphorylation
C. ATP is used for hydrolysis of a substrate bond
D. ATP is used for the new bond formation during the interaction
of two substrates ---------------E. ATP is used for a substrate
decarboxylation.
Coenzyme forms are correctly matched to vitamins except one.
Point out it:
A. Biotin carboxylated biotin
B. Vitamin B1 - ATP --------------C. Niacin NAD+ + NADP+
D. Vitamin B2 FMN + FAD
E. Pantothenic acid CoASH
Enzymes mediating transfer of a structural fragment from one
molecule to another are:Transferases
--------------------OxidasesLyases
Peptidases
Ligases
Which bond is cleaved by Alpha amylase in oral cavity?
Alpha 1-4 glycosidic ------------------Alpha 1-6 glycosidicBeta
1-4 glycosidicBeta 1-6 glycosidic
Ester bond in any ester structureWhich of the following is the
reaction that is catalyzed by lyase:
Dehydration
Oxidation
Oxidative decarboxylation
Hydrolysis --------------Acetylation
All biological catalysts are not proteins This statement is
justified by this notion:
All enzymes do not follow the Michaelis Menten hypothesis
RNAs can act as ribozymes --------------Antibodies take part in
the catalysis of many reactions
Metal ions are involved in attachment to enzymes
Enzyme activity may be controlled by hormones
LDH1 and LDH2 levels are raised in the following organ
damage
Heart, RBC, kidney ----------------------Heart, kidney,
liver
Liver, brain, kidney
Brain, heart, liver
Brain, bones, liver
Name, please, the principle base used for the classification of
enzymes:
Type of chemical reaction catalyzed by enzyme ---------Chemical
structure of enzyme
Type of energy conversion
Chemical structure of non-protein part of the enzyme
Chemical structure of products for enzymatic reaction
Name the vitamins whose derivatives are used for the formation
of oxidoreductase structure:
B2, B3B6, B9C, P
A, E
H, D
Chymotrypsin is the proteolytic enzyme catalyzing the cleavage
of peptide bonds in any protein molecule. Name the class of this
enzyme:Oxidoreductase
Isomerase Lyase
Ligase
Hydrolase --------------------The active centre of simple enzyme
is composed from:
The cofactor and prosthetic group
Linear fragment of polypeptide chain
Some amino acid residues of polypeptide chain placed in the same
spatial fragment -----------------One polypeptide chain
completely
The terminal amino acid residues
The pancreatic amylase is in need to cleave the
alpha-1.4-glycosidic bonds in the structure of polysaccharides
using the water as the substrate. Specify the class of this
enzyme:
A. Isomerase
B. Ligase
C. Lyase
D. Hydrolase -------------E. Oxido reductase
The relative group specificity may be found for enzymes
catalyzing the digestion of proteins in GIT. Find out their trivial
name:
Protein kinase ---------------Protein phosphatase
Peptidase
Transaminase
Urease
Researchers isolated five isozymes of Lactate dehydrogenase from
human blood serum and studied their properties. What property of
these isozymes indicates that they are genetic forms of the same
enzyme?
They have the same molecular weight
They catalyze the same reaction*
The same tissue localization
The same electrophoretic mobility
The same net charge of the molecule
In case of enterobiasis acrihine - the structural analogue of
vitamin B2 - is administered. The synthesis disorder of which
enzymes does this medicine cause in microorganisms?
FAD-dependent dehydrogenases
-----------------Cytochromeoxidases
Peptidases
NAD-dependet dehydrogenases
Aminotransferases
In clinical practice tuberculosis is treated with izoniazid
preparation that is an anti-vitamin able to penetrate into the
tuberculosis bacillus. Tuberculostatic effect is induced by the
interference with replication processes and oxidation-reduction
reactions due to the buildup of pseudo-coenzyme:
FMN
NAD
CoQ
FAD
TDP
Lesson 5 Module 1
.
E. Fisher`s theory explains the mechanism of enzyme action with
the fixed type of specificity, only. Name it:
A. Absolute --------------B. Absolute group
C. Absolute relative
D. Relative group
E. Stereochemical
There are some factors influencing enzyme activity. Point out
one of them resulting in complete loss of enzymatic activity:
A. Vitamin H
B. Oxygen
C. t0 C = 1000 C ----------------D. P =101325 Pa
E. Sodium chloride solution
Choose the factor that changes the cytoplasmic enzyme
conformation mainly:
A. Suicide inhibitor
B. Environmental pH value about 7.4
C. Environmental temperature value about 250 C
D. Allosteric inhibitor -------------------E. WaterPoint out the
way of proenzyme transformation to the active enzyme:
A. Limited proteolysis -----------------B. Dehydration
C. Decarboxylation
D. Inhibitor action
E. Vitamin non-protein part dissociation from enzyme Competitive
inhibitor always interacts with enzyme active centre. Find out the
explanation of this phenomenon:
A. Inhibitor causes the denaturation of active centre
B. Inhibitor is similar to a substrate structure -----------C.
Inhibitor is an exact copy of a substrate structure
D. Inhibitor is similar to the product's structure
E. Inhibitor forms a covalent type of bonds with amino acid
residues of active centreCovalent modification of inactive form of
enzyme may be catalyzed by special enzyme in a cell. Name it:
A. Esterase
B. Ligase
C. Protein kinase ---------------- D. Hydroxylase
E. Oxygenase
Succinate dehydrogenase catalyses the dehydrogenation of
succinate. Malonic acid
HOOC-CH2-COOH is used to interrupt the action of this enzyme.
Choose the inhibition type:
Allosteric
Competitive ----------------Non-competitive
Dephosphorylation
Limited proteolysis
Choose the name of scientists whose experiments are recognized
as the basis in understanding of induced fit theory for mechanism
of enzymatic reaction:
Michaelis L.
Menten M.
Koshland D. ----------------Fisher E.
Haldane R.
Diisopropyl phosphofluoride (DFP) reacts with serine proteases
irreversibly and therefore is:
Allosteric inhibitor ---------------Non-competitive
inhibitor
Competitive inhibitor
Affinity label inhibitorA stimulator
The common feature of an enzyme-cascade system regulation
is:
A. Feed back inhibition --------------B. Competitive
inhibition
C. Counter-regulationD. Amplification
E. Suicide inhibition
The formation of ES complex is due to various types of bonds
between E and S. Specify the type of bond, which is usually formed
between charged functional groups in this case:
A. Peptide bond
B. Hydrophobic interaction
C. Hydrogen bond
D. Donor-acceptor bond
E. Electrostatic interaction --------------The common enzymatic
reaction may be represented so: E + S ES ESEP E + P. Try to name
using this equation all the factors that can influence the rate of
this reaction:A. The concentration of a substrate, only
B. The concentration of enzyme, only
C. The concentration of a substrate, enzyme and product,
only
D. The concentration of enzyme-substrate complex, only
E. The concentration of a substrate, enzyme, product and
stability of ES-complex --------------Heme synthesis starts from
glycine and succinyl-SCoA interaction with -aminolevulinate
synthetase help. It is inhibited by the terminal metabolic product
- heme. Name the inhibition type:
A. Competitive Inhibition
B. Uncompetitive Inhibition
C. Non-competitive Inhibition
D. Limited proteolysis
E. Feedback Inhibition-------------The inhibitor influence on
the enzymatic reaction rate is investigated. The graph dependences
V - [S] without the inhibitor (1) and at the presence of the
inhibitor (2) are constructed.
Name the type of the inhibitor:
A. Competitive
B. Non-competitive ---------------C. Uncompetitive
D. Allosteric
E. Complete
The regulation of the enzymatic activity is carried out by
different ways. Point out the way that is used more often in the
regulation of key enzymes:
A. Limited proteolysis
B. Allosteric regulation ------------------------C. Activation
by Ca2+D. The change of pH medium
E. Competitive inhibition
Covalent catalysis as mechanism of enzyme catalysis was studied
in experimental works with one proteolytic enzyme. Find out it:
A. Pepsin
B. Aldolase
C. Chymotrypsin ----------------D. Decarboxylase
E. Glucoisomerase
Suicide type of inhibition is considered when:
A. The inhibitor structure is similar to substrate one
B. The product of reaction is the allosteric inhibitor for
enzyme
C. There is the intermediate metabolite formation from the
inhibitor which tightly binds to the active centre of enzyme to
block it ----------D. The end-product of reaction binds to the
structure of the substrate to give non-soluble complex
E. The end-product of reaction is not removed from the
environment
Choose the method that is more often used for the determination
of inhibitor type:
A. Nuclear magnetic resonance method
B. Michaelis-Menten graphical method
C. Briggs-Haldane graphical method
D. Lineweaver-Burk graphical method------------E. Eadie-Hofstee
graphical method
Find out the irreversible type of enzyme inhibition:
A. Competitive
B. Noncompetitive
C. Uncompetitive
D. Allosteric
E. Suicide ---------------Point out the activator used for the
determination of amylase activity:
A. CuSO4B. NaCl ---------------C. H3PO4D. ATP
E. Ca2+ The majority of key enzymes contain the allosteric
centre. Specify a role of this centre:
A. It attaches the substrate ----------B. It attaches the
regulatory factor
C. It changes the structure of the substrate
D. It promotes the dissociation of a coenzyme
E. It blocks the active centre
Glycogen phosphorylase b is transformed to the active form a by
the action of special kinase with the use of ATP as donor of
phosphate group. Find out, please, the type of enzyme
activation:
A. Limited proteolysis
B. Covalent modification----------------------C. Activation by
Ca2+D. The change of pH medium
E. Competitive inhibition
Sulfonamides are used as drugs to protect our organism from some
bacteria. Enzyme in bacterial cell producing folic acid from
para-aminobenzoate is inhibited by this group of drugs. Choose the
type of inhibition for Sulfonamides:
A. Competitive ----------------- B. Noncompetitive
C. Uncompetitive
D. Allosteric
E. Suicide
Name, please, the inhibitor for salivary amylase:
A. Copper sulfate ----------------- B. Sodium chloride
C. Potassium cyanide
D. Alanine
E. Hydrogen peroxide
Name the kinetic index that is changed under the influence of
competitive inhibitor on enzyme:
A. Michaelis constant
B. The initial velocity of enzymatic reaction ----- C. The
maximal velocity of enzymatic reaction
D. The dissociation constant of enzyme-substrate complex
(ES)
E. The rate constant for the formation of ES
Find out, please, the factor used to change the charge of
functional groups both in the active centre of enzyme and in the
substrate molecule:
The temperature of environment
The pH of environment ------------------The addition of
competitive inhibitor to the environment
The addition of activator to the environment
All the factors proposed may be in need
The affinity of enzyme molecule to substrate one may be
estimated using the value of:
pH of the environment
The temperature
Km for the enzyme -----------------Vmax for reaction
duration
The initial velocity of the reaction
Name, please, the equation for V-[S] dependence for the moment
of complete saturation of all the active centers of enzyme
molecules:
V=Vmax[S]/Km+[S] ----------V= kVmax
V=Vmax/Km+[S]
V=Vmax
V=k [S]
Cholesterol synthesis is regulated by feed-back mechanism. Name
the allosteric inhibitor of key enzyme for this synthesis:
ATP
Cholesterol --------------Glucose
ADP
NADPH
Salivary amylase activity may be decreased by:
The change of pH from 6,8 to the value 5,5
The decrease of temperature from 38C to 25C
The addition of copper sulfate
The increase of temperature from 38C to 65C
All the changes described may be in need --------------Name,
please, the factors that must be in constant levels during the
investigation of enzyme concentration influence the velocity of
enzymatic reaction:
pH of the environment The temperature
Substrate concentration
Activator concentration
All the factors proposed must be in constant levels
-------Lesson 6 Module 1
Point out the activator, used for the determination of urine
amylase activity under Volgemut's method:
A. CuSO4B. NaCl ----------C. H3PO4D. ATP
E. Ca2+Patient's amylase activity in the urine excesses the
normal values in ten times as much. Point out the possible
diagnosis:
A. Viral hepatitis
B. Diabetes mellitus
C. Sharp pancreatitis ---------------D. Influenza
E. Angina
Find out the term for unit of enzyme activity that is estimated
as the number of molecules of a substrate catalyzed upon in a
period 1 second by a single enzyme molecule:
A. Total activity
B. Specific activity
C. Turnover number
D. Katal ----------------E. The Unit of an enzyme activity
Find out the substrate used for amylase activity determination
in the urine of patient:
A. Glucose
B. Pyruvate
C. Maltose
D. Glycogen
E. Starch ---------------Find out the method for separation of
isozymes to determine their content in the blood serum of
patient:
A. Dialysis
B. Electrophoresis ---------------C. Spectrophotometry
D. Gel chromotography
E. Salting-out
There is the treatment of patients with achlorhydria (the
absence of free hydrochloric acid in the gastric juice of patient)
by enzyme as a drug. Name it:
A. Rennin
B. Pyruvate
C. Pepsin -------------------D. Trypsin
E. Chymotrypsin
Choose the enzyme used as diagnostic reagent for glucose content
determination in the blood:
A. Glucose-6-phosphatase
B. Pyruvate kinase
C. Maltase
D. Glucose oxidase --------------E. Amylase
A lot of factors must be taken into account to promote methodic
requirements for the determination of the enzyme activity in
biological fluids. Choose, please, the most important from
them:
A. pH of the environment
B. Temperature of the environment
C. Substrate concentration
D. Enzyme concentration
E. All the positions placed above ---------------The
determination of Lactate dehydrogenase (LDH) isozymes content
showed the increase of LDH4 and LDH5 fractions in the patient's
blood plasma. Point out the presumable diagnosis:
A. Viral hepatitis
B. Skeletal muscle dystrophy -----------------C. Diabetes
mellitus
D. Myocardial infarction
E. Acute pancreatitis
Name, please, the reagent that is added to urine of patient to
increase the activity of amylase:
A. Sodium phosphate
B. Sodium chloride ------------------C. Copper sulfate D.
Glucose
E. Choline
Name the unit of the enzyme activity, if the reaction is carried
out by the quantity of the enzyme at a rate of 1 mol of the
substrate conversion per second:
A. Standard international unit
B. Katal -------------------C. Specific activity
D. Turnover number
E. Conditional unit of activity
Patient's amylase activity in the urine equals 16 units. Point
out the possible state for this patient:
A. There is viral hepatitis in patient
B. There is diabetes mellitus in patient
C. There is the sharp pancreatitis in patient
D. The patient is apparently healthy ------------E. There is
Angina in patient
Find out the term for unit of enzyme activity that is estimated
as the number of molecules of a substrate acted upon in a period 1
second by a single enzyme molecule:
A. Total activity
B. Special activity
C. Turnover number
D. Katal -------------------E. Unit of an enzyme activity
Pancreatine is proposed as the drug to promote the normal
digestion of proteins in the small intestine of patients with
chronic pancreatitis. Choose the enzyme that is the component of
this drug and is possible to destroy protein structure:
A. Amylase
B. Lipase
C. Pepsin
D. Trypsin -----------------E. Maltase
Competitive inhibitors of enzymes may be used as drugs. Try to
find out the medicine that is used to decrease the rate of folic
acid synthesis from para-aminobenzoic acid in microorganisms which
can cause the inflammation state of tissues in humans:
A. Antimycin A
B. Pancreatine
C. Phenobarbital
D. Sulfonamide -------------------------E. Phosphogluconate
Enzyme deficiency in patient usually is discussed as severe form
of pathology because:
A. It is genetic disorder that is difficult to treat --B. It is
secondary reason of pathology
C. It is difficult to determine it
D. It cannot be prevented in the prenatal period of organism
development
E. It can be discovered in adults, only
We cannot use the enzymes as medicines for oral administration
because oral dose of enzyme:
A. Causes the allergic reactions in human organism
B. Stimulates the production of albumins by the liver
C. Can lead to the cleavage of blood plasma proteins
D. Is digested in gastrointestinal tract ------------E. Changes
the acid-alkaline balance in the blood
The decrease of Choline esterase activity in the blood serum of
patient is the signal to care for the function of one organ mainly.
Name it:
A. Liver ------------------B. Spleen
C. Brain D. Kidney
E. Pancreas gland
The principle of the method for Choline esterase activity
determination is based on the ability of the product for the
reaction catalyzed by this enzyme to change the pH of the
incubation phase. Try to give the name of this product:
A. Choline
B. Serum Albumin
C. Acetyl choline
D. Phosphatidyl choline
E. Acetic acid -------------------Genetic disorder associated
with enzymatic pathology may be caused by the:
A. Deficiency of the non-protein part of enzyme, only
B. Disorder in the regulation of the transcription of mRNA for
enzyme synthesis ---------------C. The damage of the feed-back
mechanism of enzyme regulation
D. Super-activation of inducer synthesis that is used to
stimulate transcription of mRNA for enzyme
E. All the reasons described are right
Find out, please, the value for amylase activity in the urine
(Volgemut`s method) corresponding the pathological state - acute
pancreatitis:
16 units
2 units
160 units ------------------32 units
8 units
Find out the type of Lactate dehydrogenase (LDH) isozymes whose
activity is in high level in the blood plasma of patients at
myocardium infarction:
LDH4 and LDH5LDH3, only
LDH2 and LDH3LDH1, only ------------------LDH5, only
The Acidic Phosphatase activity is determined in the blood serum
of patients with this pathologic state. Name it:
Atherosclerosis of blood vessels
Myocardium infarction
Prostatitis -------------------Acute pancreatitis
Renal insufficiency
Point out the proteolytic enzyme of the blood that helps to
solvate the fibrin clot:
A. Plasminogen
B. Lysokinase
C. Plasmin -------------------D. Antifibrinolysinogen
E. Thromboplastin
Profuse foam appeared when dentist put hydrogen peroxide on the
mucous of the oral cavity. What enzyme caused such activity?
Catalase*
Cholinesterase
Acetyltransferase
Glucose-6-phosphatdehydrogenase
Methemoglobinreductase
Twelve hours after an accute attack of retrosternal pain a
patient presented a jump of aspartate aminotransferase activity in
blood serum. What pathology is this deviation typical for?
Myocardium infarction *
Viral hepatitis
Collagenosis
Diabetes mellitus
Diabetes insipidus
Marked increase of activity of -forms of CPK (creatine
phosphokinase) and LDH-1 were revealed on the examination of the
patient's blood. What is the most likely pathology?
Miocardial infarction*
Hepatitis
Rheumatism
Pancreatitis
Cholecystitis
A patient presents high activity of LDH1, LDH2, aspartate
aminotransferase, creatine phosphokinase. In what organ (organs) is
the development of a pathological process the most probable?
In the heart muscle (initial stage of myocardium
infarction)*
In skeletal muscles (dystrophy, atrophy)
In kidneys and adrenals
In connective tissue
In liver and kidneys
During metabolic process active forms of the oxygen including
superoxide anion radical are formed in the human body. With help of
what enzyme is this anion inactivated?
Superoxide dismutase*
Catalase
Peroxidase
Glutathione peroxidase
Glutathione reductase
6 hours after the myocardial infarction a patient was found to
have elevated level of lactate dehydrogenase in blood. What isozyme
should be expected in this case?
A. LDH4B. LDH1*
C. LDH5D. LDH3E. LDH2 Lesson 7, Module 1
Nucleoside triphosphate is formed in Krebs Cycle. Point out its
abbreviation:
A. ATP
B. CTP
C. GTP ----------------D. UTP
E. TTP
Only one dehydrogenase of Krebs Cycle has the non-protein part
FAD. Name it:
A. Isocitrate dehydrogenase
B. -Ketoglutarate dehydrogenase
C. Malate dehydrogenase
D. Succinate dehydrogenase --------------E. Pyruvate
dehydrogenase
Vitamin B1 (coenzyme TPP) is necessary for only one
dehydrogenase function in Krebs Cycle. Point out it:
A. Malate dehydrogenase
B. -Ketoglutarate dehydrogenase -----------C. Isocitrate
dehydrogenase
D. Succinate dehydrogenase
E. Lactate dehydrogenase
Two reactions of Krebs Cycle are named as oxidative
decarboxylation. Point out the enzyme for this type of
reaction:
A. Citrate synthase
B. cis-Aconitate hydratase
C. Isocitrate dehydrogenase -------------------D. Succinate
dehydrogenase
E. Succinyl~SCoA synthase
Name, please, the class of organic compound usually used as
energy source for anabolic pathways in humans:
A. Monosaccharides
B. Alcohols
C. Carboxylic acids
D. Nucleosides
E. Nucleoside triphosphates -------------Name, please, the
process that is considered as the second phase of catabolic
pathways in humans:
A. Gluconeogenesis
B. Glycolysis --------------C. Urea cycle
D. Krebs cycle
E. Proteolysis
Choose, please, the transformation of intermediate metabolites
of Krebs cycle required the function of multienzyme complex:
A. Citratecis-aconitate
B. Malate oxaloacetate
C. Isocitrate alpha-ketoglutarate
D. Alpha-ketoglutarate succinyl-CoA ----------E. Fumarate
malate
Name, please, the conversion of Krebs cycle regulated by
inhibitor malonic acid
A. Succinyl-CoAsuccinate
B. Malate oxaloacetate
C. Isocitrate alpha-ketoglutarate
D. Succinatefumarate --------------E. Fumarate malate
Find out, please, the enzyme whose activity is inhibited under
the accumulation of ATP in the matrix of mitochondria:
A. Aconitase
B. Malate dehydrogenase
C. Citrate synthase --------------D. Alpha-ketoglutarate
dehydrogenase
E. Fumarase
How many stages are considered in catabolic pathway for glucose
up to the terminal products (carbon dioxide and water):
A. Two
B. Three -------------C. One
D. Four
E. Five
Name, please, the key metabolite that may be formed in catabolic
pathway both for glucose and palmitic acid in aerobic condition,
only:
A. Pyruvate
B. Oxaloacetate
C. Acetyl-CoA -----------------D. Lactate
E. Malate
Name, please, the process that is anabolic pathway in human
organism:
A. Gluconeogenesis ----------------B. Glycolysis
C. Fatty Acid Oxidation
D. Krebs cycle
E. All the proposed
Name, please, the initial substrates for Krebs cycle (first
reaction):
A. Pyruvate and oxaloacetate B. Oxaloacetate, only
C. Acetyl-CoA and oxaloacetate ---------------D. Lactate and
acetyl-CoA
E. Citric acid, only
Mg2+ and Mn2+ are in need for the function of one enzyme from
this register, only. Point out it:
A. Succinate dehydrogenase
B. Malate dehydrogenase
C. Isocitrate dehydrogenase ------------D. Aconitase
E. Fumarase
Find out the competitive inhibitor for succinate
dehydrogenase:
Malonic acid --------------Malic Acid
Fumaric acid
Citric Acid
Magnesium ion
Krebs cycle does not occur in:
Skeletal Muscle
Heart
RBC -------------Liver
All the above
Fluroacetate inhibits:
Citrate synthetase
Cis-Aconitase ------------------Succinate dehydrogenase
Alpha-ketoglutarate dehydrogenase
All these metabolic pathways or processes take place inside the
mitochondria except:
Glycolysis
Krebs cycle
Urea cycle
Oxidative phosphorylation
Fatty acid -oxidation ----------------Number of NADH molecules
produced in Citric Acid Cycle is:
2
3 ----------------------4
5
6
Name substances which are really terminal products for catabolic
pathways and for human organism:
Uric acid and Urea -------------------Carbon dioxide and
Water
ATP and Carbon dioxide
A mino acids and Keto-acids
Bilirubin and Urea
Exogenous substances may be involved in catabolic pathways to be
used as energy sources for humans EXCEPT:
Vitamins
Monosaccharides
Amino acids
Fatty acids
Alcohols -----------------------The accumulation of NADH in the
matrix of mitochondria is the signal to inhibit:
Citrate lyase
Cis-Aconitase
Isocitrate dehydrogenase -----------------Fumarase
Malate dehydrogenase
Amphybolic process must include intermediate metabolites which
are involved in both anabolic and catabolic pathways of a cell.
Choose those one:
Glycolysis
Hexose Monophosphate Shunt
Citric Acid Cycle ----------------Malate-aspartate shuttle
system
All the proposed
Energy production is due to catabolic pathways only. Name those
one:
Gluconeogenesis
Citric Acid Cycle ---------------Fatty Acid Elongation
Hexose Monophosphate Shunt
Glycogenesis
Propose the correct continuation of the phrase: Citric Acid
Cycle is:
The main producer of reduced forms of coenzymes
Anabolic process
Placed in cytoplasm of a cell
The main producer of energy for erythrocytes
Tissue respiration phase III -----------------How many moles of
high energy bond containing compound are produced due to substrate
phosphorylation in one round of Citric Acid Cycle:
Twelve ----------------Two
One
Three
Four
The rate limited step for Citric Acid Cycle duration is the
reaction catalyzed by:
Citrate synthase
Cis-Aconitase
Isocitrate dehydrogenase
Alpa-ketoglutarate dehydrogenase
Malate dehydrogenase
Oxidative decarboxylation reactions occur two times in Citric
Acid Cycle, but the mechanism of these reactions is not the same.
Choose the conversion that may be named as oxidative
decarboxylation and catalyzed by multienzyme system:
Citrate is converted to Cis-Aconitate
Isocitrate is converted to Alpa-ketoglutarate
Alpa-ketoglutarate is converted to Succinyl-CoA ---------Malate
is converted to Oxaloacetate
Succinate is converted to Fumarate
Name the regulatory enzyme from Citric Acid Cycle whose activity
is stimulated by allosteric activator ADP at condition of its
accumulation in the matrix of mitochondria:
Citrate synthase
Cis-Aconitase
Isocitrate dehydrogenase
----------------------Alpa-ketoglutarate dehydrogenase
Succinate dehydrogenase
Krebs Cycle is the stage of catabolic ways in the organism.
Point, please, the number of stage, which is corresponded to Krebs
Cycle:
1
2
4
3 ----------------------------5
Krebs cycle is regulated by the ATP/ADP ratio in aerobic cell.
Point out the value of this ratio that causes the stimulation of
Krebs Cycle duration:
0.5 --------------------1
3
2.5
5
Isocitrate was used as an oxidized substrate in the experiment
with isolated mitochondria. Specify the substance that can inhibit
the isocitrate oxidative decarboxylation:
ADP
Glucose
ATP --------------------Citrate
cAMP
Name, please, the enzyme from Krebs cycle catalyzing the
substrate phosphorylation:
. Succinyl-CoA thiokinase ----------------------. Fumarase
. Isocitrate dehydrogenase
D. Malate dehydrogenase
. Citrate synthase
The increase of one substrate concentration occurs the
mitochondrial matrix during the inhibition of Citrate synthetase in
the Krebs Cycle. Find out this substrate:
. Glucose
. Acetyl ~ SCoA --------------------------------.
(-Ketoglutarate
D. Malate
. Fumarate
Lesson 8, Module 1
Name, please, the inhibitor for complex IV of electron transport
chain:
Carbon dioxide
Potassium chloride
Hydrogen peroxide
Hydrogen sulfide ----------------Oxygen
Rotenone (the inhibitor of the first complex of the electron
transport chain) changes the P/O ratio for substrates that are
oxidized in Krebs Cycle. Choose the value of P/O at the presence of
this inhibitor per 1 mole of malate that is oxidized:
.