Question N1 Tetrameric proteins have two polypeptide chains

Answer: 0

Question N2 Most bio-molecules considered to be derived from hydrocarbons.

Answer: 1

Question N3 If the plasma pH equals to 6.7, this condition is:

Answer: Acidosis

Question N4 Which is the only amino acid with non-chiral alpha-carbon?

Answer: Glycine

Question N5 Molecules, that contain equal number of positively and negatively charged groups and
bear no net charge are called:

Answer: Zwitterions

Question N6 H2CO3 is formula of carbonic acetate

Answer: 1

Question N7 A patient whose serum pH is 7,7 is having alkalosis

Answer: 1

Question N8 Which bonds are characteristic to the secondary structure of a protein?

Answer: Hydrogen

Question N9 Regulation of water balance depends upon:

Answer: Hypothalamus

Question N11 Chemical or molecular bond that involves sharing of electron pairs between atoms is
called:

Answer: Covalent bond

Question N12 A person comes in emergency room with severe vomiting, which started about half an
hour ago and he has thrown up almost the whole gastric content, what kind of changes will appear in
pH? Explain your answer

Answer : Vomiting results in the loss of stomach acid, which contains acidic hydrogen ions (H⁺). In
cases of prolonged vomiting, the body may struggle to compensate for this loss of H⁺ ions. As a
result, the pH of the blood may become too alkaline (basic), with a relative excess of the electrolyte
bicarbonate (HCO₃⁻).

Question N13 There could be both L and D amino acids present in humans.

Answer: 1

Question N14 Renaturation is losing the structure of a protein due to environmental factors.

Answer: 0
Question N15 Which one of those system is a buffer?

Answer: All of those

Question N16 Which one is Sulfur containing amino acid:

Answer: Cysteine

Question N17 Which non-protein amino acid is involved in urea biosynthesis?

Answer: Ornithine

Question N18 The amino acids found in biological proteins are of:

Answer: 1. L-Configuration and dextro or laevoratatory

Question N19 Which amino acid does not occur in proteins of biological system?

Answer: Ornithine

Question N20 All amino acids are optically active except:

Answer: Glycine

Question N21 Which one of the following is an acidic amino acid?

Answer: Aspartic acid

Question N22 Which amino acid contains an imino group?

Answer: Proline

Question N23 Chaperone rescues proteins that have folded improperly and allows them to refold
properly

Answer: 1

Question N24 Globular proteins are multiple folding of polypeptide chain hence their shape is
ellipsoidal

Answer: 0

Question N26 Which of the following proteins can have quaternary structure?

Answer: All of the above

Question N27 Proteins, which participate in folding and shield newly synthesized polypeptides from
solvents are called:

Answer: Chaperons

Question N27 Which bonds are characteristic for tertiary structure of a protein?

Answer: ionic and hydrogen bonds, disulphide bridges , and hydrophobic and hydrophilic interactions

Question N28 The iron moves toward the plane of the Heme when O2 is bound.

Answer: 1

Question N29 Fetus and adult human have different types of Hemoglobin chains.
Answer: 1

Question N30 Myoglobin has 4 porphyrin rings inside its structure.

Answer: 0

Question N31 Inside Hemoglobin heme, iron atom is usually in a ferrous state. (Fe2 )

Answer: 1

Question N32 Which chains does Normal Adult Hemoglobin contain?

Answer: 2 alpha, 2 beta

Question N33 Hemoglobin which is NOT connected to an oxygen is called:

Answer: Deoxyhemoglobin.

Question N34 A patient is a carrier of Hemoglobin S, which disease does that patient have?

Answer: Sickle cell Anemia

Question N35 Gaining its natural structure by a protein after some damageable factors, is called:

Answer: Renaturation

Question N36 What is heme?

Answer: All of those

Question N37 Physiologic phenomenon, where Hemoglobin’s O2 binding affinity is inversely related
to acidity and concentration of CO2, is called:

Answer: Bohr’s effect

Question N38 Explain the functions of myoglobin

Answer: myoglobin is a protein found in both skeletal muscles and heart muscles, its primary
function is to supply oxygen to muscle cells. It serves as buffer of intracellular oxygen concentration
and as an oxygen reservoir in muscle.

Question N39 Define Denaturation, name the factors that could cause it.

Answer: denaturation is a process of losing the quaternary, tertiary and secondary structure of
protiens due to factors like heat, ph change, exposure to strong acidic or basic environment ,
vigorous shaking or mechanical stress and ionizing radiation.

Question N40 Biotin is a coenzyme during the hydroxylation of lysine and proline residues in collagen
synthesis

Answer: 0

Question N41 Which vitamin deficiency causes the wekness of the collagen structure and in result –
Scurvy?

Answer: Vitmain C

Question N42 Collagen is rich in:

Answer: Glycine residue

Question N43 Explain the functions of collagen

Answer:

 Structural support: provides strength and structure to your skin , muscle, bones, tendons and
ligaments
 Collagen plays important role in repairing the damaged dead skin cells
 Provides protective covering for organs
 Also contributes to blood clotting

Question N44 Nucleases catalyze the hydrolysis of proteins into their component amino acids

Answer: 0

Question N45 Enzymes lower the activation energy by stabilizing the transition state

Answer: 1

Question N46 Which of the following is the highest energy state during catalysis?

Answer: Transition state

Question N46 If increasing the substrate concentration doesn’t induce the increase of the velocity of
the reaction, it has reached its:

Answer: Maximum velocity

Question N48 Explain how competitive inhibitors work.

Question N49 State the function of hydrolases and ligases.

Question N50 Competitive inhibitors decrease the Km for the substrate

Answer: 0

Question N52 Which group of enzymes Catalyze formation of bonds between carbon and O, S, N
coupled to hydrolysis of high energy phosphates?

Answer: Lygases

Question N53 The effect of simple competitive inhibitor can be overcome by:

Answer: Raising the concentration of the substrate.

Question N53 Reversible inhibitor binds to enzyme through

Answer: Non-covalent bond.

Question N54 How do non-competitive inhibitors work?

Answer: They do not bind to an active site but still can affect the reaction rate.

Question N55 A numerically small (low) Km means:

Answer: High affinity of an enzyme for its substrate

Question N56 Vitamins: B9, cobalamin, Niacin and C are water soluble.

Answer: 1

Question N57 Non-competitive inhibitors bind to the active site of an enzyme.

Answer: 0

Question N58 Which of the following vitamins is water-soluble?

Answer: Ascorbic acid

Question N59 Which vitamin deficiency can be caused by renal failure and end up with
osteodystrophy?

Answer: Vitamin D

Question N60 Which vitamin deficiency can cause hypocoagulation (decreased blood clotting)?

Answer: Vitamin K

Question N61 A group of ribosomal RNAs, which can act as enzymes are called:

Answer: Ribozymes.

Question N63 Statin drugs that we use to treat patients with hypercholesterolemia, are:

Answer: Competitive inhibitors

Question N63 Hydrolysis of the phosphoester bond in DNA or RNA is catalyzed by:

Answer: Nucleases.

Question N64 How do competitive inhibitors work?

Answer: They are substrate analogs

Question N65 Explain how the lack of intrinsic factor can cause the pernicious anemia

Question N66 Rhodopsin is an eye pigment which contains Vitamin E protein opsin.

Answer: 0

Question N67 Parathyroid and adrenal glands play the most important roles in maintenance of
plasma calcium level.

Answer: 0

Question N68 What are Endergonic reactions?

Answer: Reactions which proceed only if free energy can be gained

Question N69 Which disease is characterized by Three Ds: Dementia, Diarrhea and Dermatitis?

Answer: Pellagra

Question N70 By chemical structure Intrinsic factor (IF) is:

Answer: Glycoprotein

Question N71 Where does the activation of blood clotting factors (By vitamin K) occur?
Answer: Liver

Question N72 ∆G‘° of the reaction A → B is 40kJ/mol under standard conditions , Write whole
information about this reaction

Question N73 Which of the following is the high energy phosphate?

Answer: All of them

Question N74 What is the name of storage polysaccharide in animals?

Answer: Glycogen

Question N74 Pick disaccharides:

Answer: Maltose, sucrose, lactose

Question N76 What is a polysaccharide? Name several examples of polysaccharides.

Question N77 Which vitamin is pantothenic acid?

Answer: Vitamin B5

Question N78 Sucrose is disaccharide consisting of:

Answer: Glucose fructose

Question N79 Polysaccharides are:

Answer: Condensation products of more than ten monosaccharide units.

Question N80 Disaccharides are:

Answer: Condensation products of 2 monosaccharide units.

Question N21 Which one of the following is an acidic amino acid?

Answer: Aspartic acid

Question N32 Which amino acid residues is iron connected to in the hemeproteins structure?

Answer: Histidin

Question N33 How may molecules of oxigen can one molecule of hemoglobin carry?

Answer: Four

Question N34 Which of them has a higher affinity to oxygen?

Answer: Myoglobin

Question N35 How does low pH affect the affinity of the hemoglobin to oxygen?

Answer: I lowers it

Question N36 Heme is cyclic tetrapyrrole cosnsisting of 4 pyrrole molecules linked by what kind of
bridges?

Answer: Methyne.

Question N37 In normal Adult Hemoglobin, iron atom is:

Answer: Ferrous

Question N38 What does posttranslational modification mean? Give an example.

Answer: PTM is a covalent process of changing a protein following a protein biosynthesis.

Question N39 Explain the cooperative binding of oxygen to hemoglobin

Question N40 Ehlers-danlos syndrome is caused by a mutation in elastin gene

Answer: 0

Question N41 Which one of the following is a fibrous protein?

Answer: Collagen

Question N42 Which of the following is the most abundant protein in the body?

Answer: Collagen

Question N43 What is the reason of pulmonary hypoplasia in patients with severe OI

Question N45 Creatine kinase is an example of oxydoreductase enzymes

Answer: 0

Question N46 Lactate dehydrogenase belongs to which main class of enzymes?

Answer: Oxidoreductases

Question N2 Anabolic reactions are exergonic reactions

Answer: 0

Question N3 Which of the following compounds is a polymer?

Answer: Triacylglycerol

Question N4 Which of the following is a monomer of proteins?

Answer: Amino acid

Question N5 Which of the following is the strongest bond?

Answer: Covalent bonds

Question N6 Van der Waals forces are significantly weaker than hydrogen bonds but potentially
extremely numerous.

Answer: 1

Question N7 pH is the negative log of the oxygen molecule concentration.

Answer: 0

Question N8 Henderson-Hasselbalch equation is an expression of

Answer: pH of a buffer

Question N9 Which of the following hormones regulate the water balance in body?
Answer: Antidiuretic hormone

Question N10 Two water molecules connect to each other with:

Answer: Hydrogen bond

Question N11 Which of the following depicts the physiological pH?

Answer: 7.4

Question N13 The only difference between amino acids is the carboxyl group.

Answer: 0

Question N14 Some amino acids could contain sulfur atoms.

Answer: 1

Question N15 Which of the following amino acids is so called ,,imino acid’’?

Answer: Proline

Question N16 Hydrophobic amino acids of transmembrane proteins are situated:

Answer: On the interior

Question N17 Losing the higher structures of a protein as a result of some chemical or physical
factors is called:

Answer: Denaturation.

Question N18 Which one of those is referred as imino acid?

Answer: Proline

Question N19 Which one of these is a feature of secondary structure of proteins?

Answer: All of those.

Question N20 Frederick Sanger was the first to identify the structure of a protein and this protein
was:

Answer: Insulin

Question N21 What’s the name of 21st amino acid?

Answer: Selenocysteine

Question N25 Which statements about allosteric enzymes is true?

Answer: The catalytic site is distinct from the allosteric site

Question N26 Which bonds stabilize the primary structure of the protein?

Answer: peptide

Question N27 Which bonds are characteristic for tertiary structure of a protein?

Question N28 Beta sheets are examples of protein’s tertiary structure

Answer: 0
Question N29 Hemoglobin has lower affinity to oxygen than myoglobin

Answer: 1

Question N30 T form of the hemoglobin is high-affinity form of it towards oxygen

Answer: 0

Question N31 Collagen is the most dominant globular protein in humans.

Answer: 0

Question N32 What contains 2 alpha chains and 2 beta chains that assume a quarternary higher
order conformation?

Answer: Hemoglobin

Question N33 Oxygen combine with hemoglobin in blood and form

Answer: Oxyhemoglobin

Question N34 Which of the following forces is favorable for protein folding?

Answer: Hydrophobic interactions

Question N35 Unfolding of a protein can be termed as

Answer: Denaturation

Question N41 Which of the following amino acid residues get hydroxylated during collagen
synthesis?

Answer: Both of them

Question N42 Which class of the collagens forms the basement membranes?

Answer: Network-forming

Question N43 Which types of posttranslational modification require Collagen synthesis?

Question N46 A cofactor in an enzymatic reaction is

Answer: Both of the above

Question N47 All the following are coenzymes except:

Answer: SGPT (ALT)

Question N48 What are the main differences between cofactors?

Question N49 Explain how non-competitive inhibitors work.

Question N51 Velocity of the reaction:

Answer: Is directly proportional of enzyme concentration

Question N56 Pellagra can be caused by niacin deficiency

Answer: 1

Point: 0.25
Question N57 Chronic alcoholism can cause severe thuamine deficiency

Answer: 1

Question N58 Hypervitaminosis A results in:

Answer: Skin disorders

Question N63 Which is the physiologically active form of vitamin D?

Answer: Calcitriol

Question N60 Pellagra can be treated with:

Answer: 1. Niacin

Point: 0.40000000000000002

Question N61 Vitamin acting as a reducing agent is:

Answer: Vitamin C

Question N66 If ΔG is zero, the system is at equilibrium and no net change takes place

Answer: 1

Question N67 Exergonic reactions are also exothermic

Answer; 1

Question N68 What is the function of Intrinsic factor?

Answer: Helps in absorption of cobalamin.

Question N69 Which vitamin does Coenzyme A have a component of its structure?

Answer: Pantothenic acid.

Question N70 Which one is Hematopoietic vitamin?

Answer: B9 and B12

Question N72 Define an exergonic reaction.

Question N74 How many high-energy phosphate groups does the ATP contain?

Answer: Two

Question N75 After the coupling of exergonic and endergonic reactions, overall energy change is:

Answer: Exergonic

Question N77 Which of the following statements is correct?

Answer: Glycogen is the storage form of glucose in human

Question N78 Which metal is held in the center of corrin ring of vitamin B12?

Answer: Cobalt

Question N79 Which of the following is a result of them niacin deficiency?

Answer: Pellagra

Question N80 Which vitamin is a precursor of FAD and FMN?

Answer: Riboflavin

Question N8 What is pH?

Answer: -log [H ]

Question N9 Which of the following statements is not correct?

Answer: Reaction of water is alkaline

Question N26 Which is not secondary protein structure?

Answer: Double helix

Question N27 Not all the proteins can have quaternary structure. Explain why

Question N28 In hemoglobin, allosteric effects occur to minimize oxygen delivery to the tissues

Answer: 0

Question N29 The major element of secondary structure in myoglobin and hemoglobin is the reverse
turn

Answer: 0

Question N30 Myoglobin consists of a single polypeptide with a prosthetic heme group?

Answer: 1

Question N31 Hemoglobin consists of a single polypeptide chain that is structurally similar to the
individual polypeptide chains of the tetrameric Myoglobin molecule

Answer: 0

Question N36 Oxygen dissociation curve of hemoglobin is shifted to right by:

Answer: Bohr effect

Question N37 Carbonmonoxide poisoning of hemoglobin leads to:

Answer: Tissue hypoxia

Question N38 May proline be used as a part of secondary structure, define why?

Question N39 What is difference between degradation and denaturation of proteins?

Question N55 In competitive inhibition:

Answer: Km increase

Question N59 B1 Deficiency can lead to:

Answer: Both A and B

Question N60 Which gland is involved in maintenance of normal blood calcium level?

Answer: Parathyroid gland

Question N63 Which water soluble vitamin has several active biochemical variations?

Answer: Vitamin B6

Question N63 Km (Michaelis constant) is:

Answer: The substrate concentration that gives one-half V-max

Question N58 Which type of inhibition is irreversible?

Answer: None of these

Question N65 What is pernicious anemia? Which tissue (other than RBC) could be damaged in this
type of anemia?

Question N71 In adults, deficiency of vitamin D causes:

Answer: Osteomalacia

Question N71 An exergonic reaction is one that:

Answer: Releases energy for work

Question N73 In exergonic reactions ΔG is:

Answer: Negative

Question N75 The branched component of starch is:

Answer: Amylopectin

Question N1 Lipids have fatty and amino acids as monomers.

Answer: 0

Question N6 Acids donate hydrogen ions in water while bases accept hydrogen ions

Answer: 1

Question N7 In the lung, the concentration of oxygen is high and hemoglobin becomes virtually
saturated with oxygen

Answer: 1

Question N23 Peptide bonds are bonds that stabilize the secondary strycture of the protein

Answer: 0

Question N24 Every protein can be renatured after being denaturated

Answer: 0

question N27 What is a lipoprotein? A Glycoprotein?

Ans: glycoprotein is ther combined form glycogen and the protein.

lipoprotein is the combined form of lipids and proteins.

Question N34 Which of them has a higher affinity to oxygen?

Answer: myoglobin

Question N33 How does low pH affect the affinity of the hemoglobin to oxygen?

Answer: I lowers it

Question N38 Define cooperative binding.

Question N39 State the structure and function of Myoglobin

Question N40 Ehlers-danlos syndrome is caused by a mutation in elastin gene

Answer: 0

Question N44 Enzymes are neither consumed nor permanently altered as the consequence of their
participation in a reaction.

Answer: 1

Question N48 Explain stereospecific properties of enzymes

Question N50 Reaction velocity will always rise with increasing the substrate concentration

Answer: 0

Question N51 Th diagnostic enzyme in muscular dystrophy is:

Answer: Creatine phosphokinase (CPK)/Creatine kinase (CK)

Question N52 High Km means:

Answer: low affinity of the enzyme to the substrate

Question N53 Which of the following inhibitors effects can be overcome by increasing the substrate
concentration?

Answer: Competitive

Question N54 Which of the following inhibitors increase the Km of the substrate and do not change
the Vmax

Answer: Competitive

Question N65 What is megaloblastic anemia?

Question N68 Which vitamin deficiency can result in rickets or osteomalacia?

Answer: Vitamin D

Question N72 How does the Gibbs free energy change during endergonic reactions?

Question N73 Which ion does ATP need to be bound to in order to be biologically active?

Answer: mg2+
Question N3 The major elements present in the human body are all the following except:

Answer: Sodium

Question N4 Which of the following is the function of mitochondria?

Answer: Oxidative phosphorylation

Question N5 If the left hand side of chemical equation is ADP water then the right hand side of that
chemical equation is equal to

Answer: AMP Pi energy

Question N6 A water molecule is an irregular, slightly skewed tetrahedron with oxygen at its center

Answer: 1

Question N7 Phosphate buffer system is most effective in intracellular medium, especially in the liver

Answer: 0

Question N10 On physiological pH, acids:

Answer: Are deprotonated

Question N11 Van der Waals forces compared to hydrogen bonds are:

Answer: Significantly weaker.

Question N13 Side chain is the only group in amino acids structure which is different for every amino
acid

Answer: 1

Question N14 Basic amino acids’ side chains are deprotonated on normal pH

Answer: 0

Question N26 Which of the following amino acids disturbs the secondary structure of proteins?

Answer: Proline

Question N28 In hemoglobin, allosteric effects occur to minimize oxygen delivery to the tissues

Answer: 0

Question N29 The major element of secondary structure in myoglobin and hemoglobin is the reverse
turn

Answer: 0

Question N30 Myoglobin consists of a single polypeptide with a prosthetic heme group?

Answer: 1

Question N43 What is the reason of pulmonary hypoplasia in patients with severe OI

Question N47 Which of the following enzyme classes catalyzes the cleavage of the bonds using water
molecule?
Answer: Hydrolases

Question N49 What is the function of lygases

It a enzyme catalysts the joinning of 2 molecules whchi forms new new bonds. It can be seen in dna
replication

Question N56 Many drugs and poisons are inhibitors of enzymes in the nervous system

Answer: 1

Question N57 The pH of a solution is determined by concentration of salt

Answer: 0

Question N58 All the following are B complex vitamins except:

Answer: Ascorbic acid

Question N59 Vitamin D3 is formed from

Answer: 7-dehydrocholesterol

Question N66 Most of the ATP made during cellular respiration is generated by oxidative
phosphorylation

Answer: 1

Question N67 ATP has the greatest amount of available energy per molecule?

Answer: 1

Question N75 What is the common metabolite that every foodstuff is broken down to?

Answer: Acetyl coA

Question N77 All the following are monosaccharides except

Answer: Maltose

Question N78 Glucose is the constituent of

Answer: 1. Starch

Question N79 Stereoisomers differ from each other in:

Answer: Spatial configuration

Question N80 Glucose and galactose are epimers which differ in orientation of H and OH on

Answer: C4

Question N33 The iron in heme is linked to globin through:

Answer: Histidine

Question N44 Competitive inhibitors resemble the structure of an enzyme.

Answer: 0

Question N72 Why do we prescribe vitamin K shots to newborn children?

Question N8 Electrostatic interaction between oppositely charged groups within a molecule is called:

Answer: Salt bridges.

Question N9 Which of the following forces participate in maintaining molecular structure?

Answer: All of those

Question N25 Bonds that stabilize the tertiary structure of the proteins, rise between:

Answer: R-groups of the amino acids

Question N46 How do enzymes affect the activation energy?

Answer: They decrease

Question N48 How does the enzyme speed up the reaction?

Question N74 What is the product of removing one phosphate group from ATP molecule?

Answer: ADP

Question N6 Acids are the molecules that disocciate into OH- and conjugate base on normal pH

Answer: 0

Question N7 Buffer systems have unlimited buffering capacity

Answer: 0

Question N15 Amino acids differ from each other by:

Answer: Side chain

Question N34 At isoelectric pH, the protein molecule has:

Answer: 1. Equal number of positive and negative charges

Question N35 Proteins are:

Answer: All of the above

Question N38 What does posttranslational modification mean? Give an example

Ans: After the translational process the proteins make some modification and form different proteins.

Glycolysation : adding sugar residue to the proteins

Methylation : adding methyl group to proteins

Acetylation : adding acetyl group to the proteins

Lipidisation : addind lipids to the proteins

Hydroxylation : adding OH group to the proteins

Question N65 Explain the role of vitamin C in tissues’ integrity

What is the function of Vitamin K? Who is at risk of having vitamin K deficiency?

Answer:It helps in blood coauglation . The new born babies are at high risk where the mother cant
provide Vitamin K sufficients through the milk .

Question N73 Anabolic reactions:

Answer: Urilize energy, so they are endergonic

Question N18 Amino acid residues commonly found in the middle of β turn are:

Answer: Pro and Gly

Question N19 A tripeptide has

Answer: 3 amino acids and 2 peptide bonds

Question N20 Peptide bond is made between:

Answer: Amino group of one amino acid and carboxylic group of another amino acid

Question N6 Antidiuretic hormone (ADH) controls the retention of water in human body.

Answer: 1

Question N7 Oxygen molecule inside the structure of water molecule is strongly electropositive.

Answer: 0

QN1:The unit of ΔS is:

Answer: 1. Joules/mole

QN2: Question N9 Which of the following statements is not correct?

Answer:
A base can accept hydroxyl ions

Question N9 Which of the following statements is not correct?

Answer:
A base can accept hydroxyl ions

7 NADH andFADH2 are reduced coenzymes? True.

8. Acetyl Coa enter the TCA cycle. True

9. During cellular respiration, most of the ATP made, is generated by oxidative phosphorylation.
True
10. The enzymes of the TCA cycle in a eukaryotic cell are located in the mitochondria. True
11. Citric acid cycle occurs in mitochondria. True
12. Most multi-cellular organisms obtain energy for the synthesis of ATP during oxidative
phosphorylation from a proton gradient across the inner mitochondrial membrane. True
13. The end product of glycolysis is pyruvate, which enters the citric acid cycle after being
converted to acetyl-CoA. True
 14. Membrane potential and the proton gradient are both required to make ATP. True
15. In electron transport, electrons ultimately pass to oxygen. True
16. 6 ATP per mole of glucose input are required for gluconeogenesis True

17. The production or break down of ATP is often coupled with the metabolic reactions of
biosynthesis and catabolism.
A. True
65.The main site for gluconeogenesis is liver
A. True
66.Gluconeogenesis uses 4 ATPs and 2 GTPs per glucose
A. True

67.Gluconeogenesis is the synthesis of glucose from non-carbohydrate precursors

A. True

68.Hydrolysis of lactose yields galactose and glucose

A. True

69. Two major products of pentose phosphate pathway are nicotinamide adenine
dinucleotide and ribose 5-phosphate

B. False

70.The conversion of pyruvate to lactate is catalyzed by lactate dehydrogenase

A. True
71.Storage polysaccharide made by animals is glycogen
A. True
72. Under aerobic condition pyruvate is converted by pyruvate dehydrogenase to acetyl
CoA
A. True
73. The ultimate source of energy that sustains living systems is sunlight
A. True
74. Glycogen has α-1,4 and α-1,6 linkages
A. True

6.Fo domain of ATP synthase protrudes in the mitochondrial matrix,F1 domain spans the
membrane and forms a proton channel...
Ans: false
8.The respiratory chain collects and transports reducing equivalents directing them to their final
reaction with oxygen to form water and liberated free energy is trapped as high energy phosphate...
Ans: true