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Тестовые задания рубежного контроля 1 для дисциплины «Bases of Biochemistry»
№ Наименование раздела
Количество
Выборка
вопросов
1
Введение в биохимию
17
5
2
Аминокислоты
14
5
3
Белки
36
5
4
Ферменты
36
5
5
Углеводы
30
5
Раздел 1.
Введение в биохимию
The history of biochemistry spans approximately ….. ago
A. 400 years
B. 600 years
C. 300 years
D. 900 years
E. 1500 years
The term "biochemistry" was proposed
A. Carl Neuberg
B. Schmidt
C. Lui Pasteur
D. Antoine Lavoisier
E. Fisher
How many chemical elements are essential for organisms?
A. about 30
B. about 90
C. about 50
D. about 20
E. about 10
Specify micronutrients are included ….
A. Zn, Mo, Cu, Fe, Co
B. Ca, Mg, Si, S, C
C. Cu, Mn, H, S, Cl
D. Zn, H, C, Fe, Cl
E. Zn, Hg, Cu, Fe, C
Specify primary macronutrients are included ….
A. O, H, C, P, N, K
B. Ca, Mg, Si, S, Cl
C. Zn, Mo, Cu, Fe, Co
D. Zn, H, C, Fe, C
E. Zn, Hg, Cu, Fe, C
Specify secondary and tertiary macronutrients are included ….
A. Ca, Mg, Si, S, Cl
B. Zn, Mo, Cu, Fe, Co
C. O, H, C, P, N, K
D. Zn, H, C, Fe, Cl
E. Zn, Hg, Cu, Fe, C
What function does provide the Ca?
A. it plays key role in the bone formation
B. it is necessary element for synthesis of chlorophyll and photosynthesis
C. it enters into composition of skin, hair and feathers
D. it enters into enzymes of all classes
E. it enters into all proteins
What function does provide the Zn?
A. it enters into enzymes of all classes
B. it plays key role in the bone formation
C. it is necessary element for synthesis of chlorophyll and photosynthesis
D. it enters into composition of skin, hair and feathers
E. it enters into only one class of enzymes
What function does provide the S?
A. it enters into composition of skin, hair and feathers
B. it enters into enzymes of all classes
C. it plays key role in the bone formation
D. it is necessary element for synthesis of chlorophyll and photosynthesis
E. it enters into all proteins
What function does provide the Mg?
A. it is a necessary element for chlorophyll synthesis and photosynthesis
B. it enters into composition of skin, hair and feathers
C. it enters into enzymes of all classes
D. it plays key role in the bone formation
E. it enters into all proteins
Non-essential amino acids
A. Tryptophan
B. alanine
C. Valine
D. Phenylalanine
Uridine - it ...
A. nucleotide
B. The nucleoside
C. nitrogenous bases
D. uracil, connected with phosphoric acid
Neutral fats - it's ...
A. glycerol esters of fatty acids
B. ethylene glycol esters of fatty acids
C. esters monatomic alcohols and fatty acids
D. esters of all alcohols and fatty acids
Oxidase enzymes
A. Catalyze the transfer of electrons (protons) from the substrate at the O2
B. Catalyze the transfer of electrons (protons) to an intermediate substrate
C. Catalyze the joining of oxygen
D. Catalyze the transfer of only 1 electron
Enzymes consist of:
a. Protein and non-protein part
b. Only protein
c. Enzyme
d. coenzyme
The hormone melatonin, which is involved in skin blanching in lower vertebrates, is released
from the
A. pineal gland
B. melanocytes.
C.anterior pituitary gland.
D. suprachiasmatic nucleus of the hypothalamus.
Beta pleated sheets are examples of protein's
A. secondary structure
B. primary structure
C. tertiary structure
D. quaternary structure
Раздел 2.
Аминокислоты.
There are ….. amino acids which participate in building of native proteins?
A. twenty two
B. twenty one
C. twenty three
D. twenty
E. twenty nine
Call proteinogenic amino acids which enter only into bacteria proteins
A. pyrrolysine and selenocysteine
B. pyrrolysine and glycine
C. selenocysteine and isoleucine
D. selenovaline and pyrrolysine
E. pyrrolysine and valine
Cysteine is structurally similar to
A. serine
B. pyrrolysine
C. histidine
D. isoleucine
E. glycine
This proteinogenic amino acid contains imidazole group
A. histidine
B. pyrrolysine
C. serine
D. isoleucine
E. glycine
These amino acids contain nonpolar side chain
A. Alanine, valine, leucine, isoleucine, glycine, methionine
B. Aspartate, glutamate
C. Serine, threonine, cysteine, asparagine, glutamine
D. Phenylalanine, tyrosine, tryptophan
E. Histidine, tyrosine
These amino acids contain second carboxyl group on its aliphatic chain
A. Aspartate, glutamate
B. Serine, threonine, cysteine, asparagine, glutamine
C. Phenylalanine, tyrosine, tryptophan
D. Alanine, valine, leucine, isoleucine, glycine, methionine
E. Histidine, tyrosine
These amino acids contain aromatic side chains
A. Phenylalanine, tyrosine, tryptophan
B. Aspartate, glutamate
C. Serine, threonine, cysteine, asparagine, glutamine
D. Alanine, valine, leucine, isoleucine, glycine, methionine
E. Histidine, tyrosine
These amino acids contain polar side chain
A. Serine, threonine, cysteine, asparagine, glutamine
B. Aspartate, glutamate
C. Phenylalanine, tyrosine, tryptophan
D. Alanine, valine, leucine, isoleucine, glycine, methionine
E. Histidine, tyrosine
These amino acids are called non-essential
A. amino acids which be able to synthesize in only human organism
B. amino acids which be able to synthesize in all animal organism
C. amino acids which all organisms obtain only in diet
D. amino acids which humans obtain only in diet
E. amino acids which plants obtain only in diet
These amino acids are called essential
A. amino acids which humans obtain only in diet
B. amino acids which be able to synthesize in only human organism
C. amino acids which be able to synthesize in all animal organism
D. amino acids which all organisms obtain only in diet
E. amino acids which plants obtain only in diet
There are …… amino acids are called non-essential for human
A. 11
B. 3
C. 9
D. 8
E. 5
There are …… amino acids are called essential for human
A. 9
B. 11
C. 3
D. 8
E. 5
An isoelectric point is the pH at which an amino acid exists primarily in its…
A. zwitterion form
B. negative charge form
C. dissoluted form
D. positive charge form
E. ion form
Peptide bond is formed between amino-acids as result …
A. condensation reaction
B. decarboxylation of amino acids
C. deamination of amino acids
D. polymerization reaction
E. isomerization reaction
Раздел 3.
Белки.
All functional proteins are called….
A. native proteins
B. complex proteins
C. simple proteins
D. essential proteins
E. non-essential proteins
The proteids are also called….
A. complex proteins
B. simple proteins
C. essential proteins
D. native proteins
E. non-essential proteins
The function of a protein is directly depended on its…..
A. three-dimensional structure
B. amino acid sequence
C. secondary protein structure
D. native proteins
E. primary protein structure
Sickle-cell anemia is a molecular disease by caused mutation of…..
A. hemoglobin
B. myoglobin
C. immunoglobulins
D. myosin
E. pepsin
The contractile force of muscle is generated by caused ….
A. myosin
B. myoglobin
C. immunoglobulins
D. hemoglobin
E. pepsin
It is a major class of antibody molecules and one of the most abundant proteins in the
blood serum
A. immunoglobulins
B. myoglobin
C. myosin
D. hemoglobin
E. pepsin
Mucoproteins contain this non-protein component
A. carbohydrate
B. lipids
C. pigments
D. nucleic acid
E. heavy metal
Chromoproteins contain this non-protein component
A. pigments
B. carbohydrate
C. lipids
D. nucleic acid
E. heavy metal
Histones are important ….
A. proteins are entered into composition of nucleic substance
B. group of plant storage proteins
C. group of egg proteins
D. group of fish sperm proteins
E. group of enzymes
Prolamins are important ….
A. group of plant storage proteins
B. proteins are entered into composition of nucleic substance
C. group of egg proteins
D. group of fish sperm proteins
E. group of enzymes
Protamines are important ….
A. group of fish sperm proteins
B. group of plant storage proteins
C. proteins are entered into composition of nucleic substance
D. group of egg proteins
E. group of enzymes
Albumins are important ….
A. group of egg proteins
B. group of fish sperm proteins
C. group of plant storage proteins
D. proteins are entered into composition of nucleic substance
E. group of enzymes
Find the definition describing the alpha helix structure
A. The polypeptide chain is coiled tightly in the fashion of a spring
B. The specific geometric shape caused by intramolecular and intermolecular
hydrogen bonding
C. The protein chains are aligned side-by-side with every other protein chain
aligned in an opposite direction
D. The series of amino acids joined by peptide bonds
E. The series of amino acids joined by hydrogen bonds
Find the definition describing the beta-pleated structure
A. The protein chains are aligned side-by-side with every other protein chain
aligned in an opposite direction
B. The polypeptide chain is coiled tightly in the fashion of a spring
C. The specific geometric shape caused by intramolecular and intermolecular
hydrogen bonding
D. The series of amino acids joined by peptide bonds
E. The series of amino acids joined by hydrogen bonds
Find the second parts of expressions about proteins
Life is …..
A. an existence of protein bodies
B. are constructed from the same set of 22 amino acids
C. can generate movement
D. are called native proteins
E. control growth and differentiation
Find the second parts of expressions about proteins
Only proteins ….
A. can generate movement
B. an existence of protein bodies
C. are constructed from the same set of 22 amino acids
D. are called native proteins
E. control growth and differentiation
Find the second parts of expressions about proteins
All functional proteins ….
A. are called native proteins
B. can generate movement
C. an existence of protein bodies
D. are constructed from the same set of 22 amino acids
E. control growth and differentiation
Find the second parts of expressions about proteins
All native proteins of the highest and lowest organisms ….
A. are constructed from the same set of 22 amino acids
B. are called native proteins
C. can generate movement
D. an existence of protein bodies
E. control growth and differentiation
Find the second parts of expressions about proteins
Many proteins …….
A. control growth and differentiation
B. are constructed from the same set of 22 amino acids
C. are called native proteins
D. can generate movement
E. an existence of protein bodies
Find the second parts of expressions about proteins
The spatial arrangement of atoms in a protein …..
A. is called its conformation
B. are proteins
C. are called native proteins
D. can generate movement
E. an existence of protein bodies
Find the second parts of expressions about proteins
Almost all enzymes …..
A. are proteins
B. is called its conformation
C. are called native proteins
D. can generate movement
E. an existence of protein bodies
Find the second parts of expressions about proteins
The fundamental alphabet of proteins …..
A. contains 20-22 building blocks
B. caused by hydrogen bonds
C. its three-dimensional structure
D. are called native proteins
E. can generate movement
Find the second parts of expressions about proteins
The function of a protein is directly dependent on …..
A. its three-dimensional structure
B. contains 20-22 building blocks
C. caused by hydrogen bonds
D. its three-dimensional structure
E. are called native proteins
Find the second parts of expressions about proteins
In the protein molecules amino acids ….
A. are joined by peptide bonds
B. 3.6 amino acid units
C. its three-dimensional structure
D. in the fashion of a spring
E. is a polypeptide chain
Find the second parts of expressions about proteins
The primary protein structure …..
A. is a polypeptide chain
B. are joined by peptide bonds
C. 3.6 amino acid units
D. its three-dimensional structure
E. in the fashion of a spring
Find the second parts of expressions about proteins
One "turn" of the coil requires ……
A. 3.6 amino acid units
B. is a polypeptide chain
C. are joined by peptide bonds
D. its three-dimensional structure
E. in the fashion of a spring
Find the second parts of expressions about proteins
The secondary protein structure is the specific geometric shape …..
A. in the fashion of a spring
B. 3.6 amino acid units
C. is a polypeptide chain
D. are joined by peptide bonds
E. its three-dimensional structure
Find the second parts of expressions about proteins
The molecular weights of most proteins…..
A. are between 5500 and 220,000
B. an alpha helix and the beta pleated sheet
C. is a polypeptide chain
D. are joined by peptide bonds
E. its three-dimensional structure
Find the second parts of expressions about proteins
There are two types of the secondary protein structure …..
A. an alpha helix and the beta pleated sheet
B. are between 5500 and 220,000
C. is a polypeptide chain
D. caused by hydrogen bonds
E. its three-dimensional structure
Find the second parts of expressions about proteins
In the alpha helix, the polypeptide chain is coiled tightly…..
A. caused by hydrogen bonds
B. an alpha helix and the beta pleated sheet
C. are between 5500 and 220,000
D. is a polypeptide chain
E. its three-dimensional structure
Find the second parts of expressions about proteins
Some proteins contain two or more …..
A. polypeptide chains, or subunits, which may be identical or different
B. from the gene sequence
C. the amino acid sequence of insulin, a protein hormone.
D. from the gene sequence
E. the amino acid sequence of insulin, a protein hormone
Find the second parts of expressions about proteins
There is a denaturation of protein ….
A. when body temperature raises
B. is a process in which the three-dimensional shape of a molecule is changed from
its native state without rupture of peptide bonds
C. protein is held together by interactions between the side chains - the "R" groups.
D. are base of some receptors work
E. are temperature, heavy metal, radiation, acids and other
Find the second parts of expressions about proteins
In 1953, Frederick Sanger determined…..
A. the amino acid sequence of insulin, a protein hormone
B. polypeptide chains, or subunits, which may be identical or different
C. from the gene sequence
D. the amino acid sequence of pepsin, a protein hormone.
E. from the protein sequence
Find the second parts of expressions about proteins
The amino acid sequence of a protein can be determined…
A. from the gene sequence
B. the amino acid sequence of insulin, a protein hormone
C. polypeptide chains, or subunits, which may be identical or different
D. from the protein sequence
E. the amino acid sequence of pepsin, a protein hormone
Find the second parts of expressions about proteins
Reasons of protein denaturation …..
A. are temperature, heavy metal, radiation, acids and other
B. when body temperature raises
C. is a process in which the three-dimensional shape of a molecule is changed from
its native state
D. protein is held together by interactions between the side chains - the "R" groups.
E. is a base of some receptors work
Find the second parts of expressions about proteins
Denaturation and renaturation of a protein….
A. is a base of work of many receptors
B. protein is held together by interactions between the side chains - the "R" groups.
C. is a process in which the three-dimensional shape of a molecule is changed from
its native state without rupture of peptide bonds
D. when body temperature raises
E. the amino acid sequence of insulin, a protein hormone
Раздел 4.
Ферменты.
Find the similarity between enzymes and inorganic catalysts
A. They reduce activation energy of reaction.
B. Enzymatic reaction rate is much high
C. High specificity
D. Soft working conditions
E. There is possibility of reaction rate regulation
Find the similarity between enzymes and inorganic catalysts
A. They do not vary a reaction direction
B. High specificity
C. Soft working conditions (into cell)
D. There is possibility of reaction rate regulation
E. Enzymatic reaction rate is proportional to quantity of enzyme
Find the similarity between enzymes and inorganic catalysts
A. They accelerate reaction equilibrium beginning, but they do not change it
B. High specificity
C. Soft working conditions (into cell)
D. There is possibility of reaction rate regulation
E. Enzymatic reaction rate is proportional to quantity of enzyme
Find the similarity between enzymes and inorganic catalysts
A. Quantity of enzyme is not consumed during the enzymatic reaction
B. High specificity
C. Soft working conditions (into cell)
D. There is possibility of reaction rate regulation
E. Enzymatic reaction rate is proportional to quantity of enzyme
Find the differences between enzymes and inorganic catalysts
A. Enzymatic reaction rate is much high
B. They catalyze only energetically possible reactions
C. They do not vary a reaction direction
D. They accelerate reaction equilibrium beginning, but they do not change it
E. Quantity of enzyme is not consumed during the enzymatic reaction.
Find the differences between enzymes and inorganic catalysts
A. High specificity
B. They catalyze only energetically possible reactions
C. They do not vary a reaction direction
D. They accelerate reaction equilibrium beginning, but they do not change it
E. Quantity of enzyme is not consumed during the enzymatic reaction.
Find the differences between enzymes and inorganic catalysts
A. Soft working conditions
B. They catalyze only energetically possible reactions
C. They do not vary a reaction direction
D. They accelerate reaction equilibrium beginning, but they do not change it
E. Quantity of enzyme is not consumed during the enzymatic reaction.
Find the differences between enzymes and inorganic catalysts
A. There is possibility of reaction rate regulation
B. They catalyze only energetically possible reactions
C. They do not vary a reaction direction
D. They accelerate reaction equilibrium beginning, but they do not change it
E. Quantity of enzyme is not consumed during the enzymatic reaction.
Find the differences between enzymes and inorganic catalysts
A. Enzymatic reaction rate is proportional to quantity of enzyme
B. They catalyze only energetically possible reactions
C. They do not vary a reaction direction
D. They accelerate reaction equilibrium beginning, but they do not change it
E. Quantity of enzyme is not consumed during the enzymatic reaction.
Find the second parts of expressions about enzymes
Simple enzyme require no chemical groups for activity other…..
A. than their amino acid residues
B. one or several protein subunits in their structure
C. are proteins
D. covalently bound to an enzyme
E. a holoenzyme
Find the second parts of expressions about enzymes
There are enzymes containing…..
A. one or several protein subunits in their structure
B. than their amino acid residues
C. are proteins
D. covalently bound to an enzyme
E. a holoenzyme
Find the second parts of expressions about enzymes
Enzymes.....
A. are proteins
B. one or several protein subunits in their structure
C. than their amino acid residues
D. covalently bound to an enzyme
E. a holoenzyme
Find the second parts of expressions about enzymes
Prosthetic group is a metal or other co-enzyme ……
A. covalently bound to an enzyme
B. are proteins
C. one or several protein subunits in their structure
D. than their amino acid residues
E. a holoenzyme
Find the second parts of expressions about enzymes
Holoenzyme is a complete, catalytically active enzyme….
A. including all co-factors
B. a holoenzyme
C. where catalysis occurs
D. are coenzymes
E. their substrates
Find the second parts of expressions about enzymes
Apoenzyme is a protein portion of……
A. a holoenzyme
B. including all co-factors
C. where catalysis occurs
D. are coenzymes
E. their substrates
Find the second parts of expressions about enzymes
Active site is a region of an enzyme comprised of different amino acids…..
A. where catalysis occurs
B. a holoenzyme
C. including all co-factors
D. are coenzymes
E. their substrates
Find the second parts of expressions about enzymes
Many vitamins......
A. are coenzymes
B. where catalysis occurs
C. a holoenzyme
D. including all co-factors
E. their substrates
Find the second parts of expressions about enzymes
Enzymes are specific to......
A. their substrates
B. are coenzymes
C. where catalysis occurs
D. a holoenzyme
E. including all co-factors
Find the second parts of expressions about enzymes
The enzyme specificity is determined....
A. by the active site
B. their substrates
C. are coenzymes
D. where catalysis occurs
E. including all co-factors
Apoenzyme is a ….
A. protein part of enzyme
B. apoprotein
C. inorganic ions
D. prosthetic group
E. organic group
Cofactor is a ….
A. inorganic ions
B. apoprotein
C. protein part of enzyme
D. prosthetic group
E. organic group
Organic molecule is a ….
A. prosthetic group
B. inorganic ions
C. apoprotein
D. protein part of enzyme
E. organic group
Active site is a ….
A. combination of the amino acid residuals
B. protein part of enzyme
C. non-protein part of enzyme
D. apoprotein part of enzyme
E. combination of the protein residuals
Allosteric site …
A. controls activity of enzymes
B. provides connecting with a substrate
C. provides reaction realization
D. provides formation of enzyme-substrate complex
E. provides formation of enzyme-product complex
Catalytic site …
A. provides reaction realization
B. controls activity of enzymes
C. provides connecting with a substrate
D. provides breaking of enzyme-product complex
E. provides formation of enzyme-product complex
Multienzyme complex contains
A. several different enzymes
B. different variants of the same enzyme having identical functions
C. several allosteric sites
D. several active sites
E. several unchor centers
Isozymes are
A. different variants of the same enzyme having identical functions
B. several allosteric sites
C. several active sites
D. several different enzymes
E. several unchor centers
Lyases provide….
A. addition of groups to double bonds, or formation of double bonds by removal of
groups
B. transfer of electrons or hydride ions
C. transfer of groups within molecules to yield isomeric forms
D. formation of COC, COS, COO, and CON bonds by condensation reactions
coupled to ATP cleavage
E. isomerisation of substrate
Ligases provide….
A. formation of COC, COS, COO, and CON bonds by condensation reactions
coupled to ATP cleavage
B. addition of groups to double bonds, or formation of double bonds by removal of
groups
C. transfer of electrons or hydride ions
D. transfer of groups within molecules to yield isomeric forms
E. isomerisation of substrate
Enzymes are classified
A. by the reactions they catalyze
B. by the active site structure
C. by the enzyme structure
D. by the substrate
E. by the co-factor
Eenzymes display different specificity
A. stereospecifity, absolute, group specificity
B. individual, group , substrate specificity
C. individual, absolute, substrate specificity
D. individual, group specificity
E. individual, absolute, optical specificity
Stereospecifity –
A. it catalyzes only one of stereoisomers
B. it catalyzes of substrates with the general structural features
C. it catalyzes only one substrate
D. it catalyzes only two substrate
E. it catalyzes of substrates with the different structural features
Group specificity –
A. it catalyzes of substrates with the general structural features
B. it catalyzes only one of stereoisomers
C. it catalyzes only one substrate
D. it catalyzes only two substrate
E. it catalyzes of substrates with the different structural features
Absolute specificity –
A. it catalyzes only one substrate
B. it catalyzes of substrates with the general structural features
C. it catalyzes only one of stereoisomers
D. it catalyzes only two substrate
E. it catalyzes of substrates with the different structural features
Define the type of describing catalytic mechanism
There are specific amino acid residues in an enzyme active site which are good donors
or acceptors of protons.
A. Acid-base catalysis
B. Covalent catalysis
C. Binding energy catalysis
D. Metal ion catalysis
E. Acid catalysis
Define the type of describing catalytic mechanism
Enzymes react with the substrates, forming enzyme-substrate complex by covalent
bonds
A. Covalent catalysis
B. Acid-base catalysis
C. Binding energy catalysis
D. Metal ion catalysis
E. Acid catalysis
Раздел 5.
Углеводы.
Content of carbohydrates in a human body and animals is about
A. 2 %
B. 4 %
C. 80 %
D. 90 %
E. 25 %
Content of carbohydrates in plants
A. 80 %
B. 2 %
C. 4 %
D. 90 %
E. 25 %
What organisms are capable to synthesize carbohydrates
A. only plants and some microorganisms
B. some plants and microorganisms
C. some plants and animals
D. only plants
E. only some microorganisms
For the first time the term «carbohydrates» was offered by
A. Schmidt
B. Antoine Lavoisier
C. Carl Neuberg
D. Lui Pasteur
E. Fisher
Carbohydrates are …..
A. polyols with aldehydic or ketonic group on their structure and their derivatives
B. aldehydic or ketonic and their derivatives
C. polyaldehydic or polyketonic and their derivatives
D. polyols with carboxyl group on their structure and their derivatives
E. polymers and their derivatives
According to modern classification carbohydrates are subdivided into three basic
groups
A. 3 groups
B. 5 groups
C. 4 groups
D. 2 groups
E. 9 groups
Aldoses and ketoses are divided according to number of carbon atoms in a molecule
A. trioses, tetroses, pentoses, hexoses etc.
B. Monosaccharoses, oligosaccharides, polysaccharides
C. disaccharides, trisaccharides etc.
D. homopolysaccharides, heteropolysaccharides
E. galactose, glucose, fructose
Oligosaccharides are subdivided into…
A. disaccharides, trisaccharides etc.
B. Monosaccharoses, oligosaccharides, polysaccharides
C. trioses, tetroses, pentoses, hexoses etc.
D. homopolysaccharides, heteropolysaccharides
E. galactose, glucose, fructose
Sucrose is a disaccharide in which
A. the glucose and fructose residual is connected by α1,2- glycosidic bound
B. the galactose residual is connected to glucose by β1,4- glycosidic bound
C. the glucoses residuals are connected by β1,4 - glycosidic bound
D. contains α-1,4 and α - 1,6-glycosidic bounds, has mass not less than 1 million
E. the fructoses residuals are connected by α1,2- glycosidic bound
Lactose is milk sugar in which
A. the galactose residuals are connected to glucose by β1,4- glycosidic bound
B. the glucose and fructose residuals are connected by α1,2- glycosidic bound
C. the glucoses residuals are connected by β1,4 - glycosidic bound
D. contains α-1,4 and α - 1,6-glycosidic bounds, has mass not less than 1 million
E. the fructoses residuals are connected by α1,2- glycosidic bound
It is a store polysaccharide of animal tissues
A. Glycogen
B. Cellulose
C. Dermatan
D. Chondroitin sulfate
E. Starch
It is an important structural component of cartilage and provides much of its resistance
to compression
A. Chondroitin sulfate
B. Cellulose
C. Glycogen
D. Dermatan
E. Starch
It is a glycosaminoglycans (it is also called a mucopolysaccharide) found mostly
in skin, but also in blood Vessels, heart valves, tendons, and lungs
A. Dermatan
B. Cellulose
C. Glycogen
D. Chondroitin sulfate
E. Starch
It is a plant polysaccharide which has fibrillar structure
A. Cellulose
B. Glycogen
C. Chondroitin sulfate
D. Starch
E. Dermatan
Find example describing hydroosmotic function of carbohydrates
A. heteropolysaccharides possess high hydrophilic property and, thus, keep Н2О
and provide a skin turgor
B. cellulose builds walls of plant cells
C. chondroitin sulfates enter to composition of connective tissues
D. it is a basic material of rubbing surfaces of joints
E. heparin is a cofactor of the lipoprotein lipase
Find example describing electroisolating function of lipids
A. they are isolating material in myelin sheath of nerves
B. some lipids are solvents for others
C. they are emulsifying agents, that is stabilize water-oil emulsions
D. hypodermic fat is a good thermo protection
E. hypodermic fat provides mechanical protection of an internals
According to modern classification carbohydrates are subdivided into three basic
groups by their ……
A. Structure
B. Composition
C. Functions
D. Properties
E. Chemical activity
Most common monosaccharides have ……
A. 3 to 6 carbon atoms
B. 3 to 5 carbon atoms
C. 5 to 6 carbon atoms
D. 3 to 10 carbon atoms
E. 6 to 10 carbon atoms
Triose contains
A. 3 carbons
B. 4 carbons
C. 5 carbons
D. 6 carbons
E. 7 carbons
Tetrose contains.
A. 4 carbons
B. 3 carbons
C. 5 carbons
D. 6 carbons
E. 7 carbons
Pentose contains
A. 5 carbons
B. 4 carbons
C. 3 carbons
D. 6 carbons
E. 7 carbons
Hexose contains
A. 6 carbons
B. 4 carbons
C. 3 carbons
D. 5 carbons
E. 7 carbons
It is a primary carbohydrate our bodies use to produce energy
A. Glucose
B. Starch
C. Cellulose
D. Fructose
E. Dermatan
It is a primary carbohydrate our brain use to produce energy
A. Glucose
B. Starch
C. Cellulose
D. Fructose
E. Dermatan
In our bodies all carbohydrates are converted into ……
A. Glucose
B. Starch
C. Cellulose
D. Fructose
E. Dermatan
This carbohydrate is a part of the nucleotides of DNA
A. deoxyribose
B. Glucose
C. Cellulose
D. Fructose
E. ribose
This carbohydrate is a part of the nucleotides of RNA
A. ribose
B. deoxyribose
C. Glucose
D. Cellulose
E. Fructose
Sucrose is a
A. disaccharide
B. polysaccharide
C. monosaccharide
D. triose
E. tetrose
Starch is made of ....
A. a glucose molecules
B. a fructose molecules
C. a galactose molecules
D. a triose molecules
E. a tetrose molecules