BIOCHEMISTRY: EXERCISES

1. Differentiate the following biochemical terms and explain their physiological

importance in the functioning of the human body by giving at least 1 example
of each term:
Anabolism and Catabolism

Catabolism: It is the process of breaking down (degradation) of the big

molecules (polymers or macromolecules) into the small molecules (monomers).
This degradation helps for example in digestion (absorption) where the small
molecules can enter the cells; in the cytoplasm some monomers can be breaken
down into the smallest molecules depending on the needs of the body (glucose
can be transformed into pyruvic acid by glycolysis).

Anabolism: It is the biochemical process of synthesis of the macromolecules

from the small molecules. This process helps in formation of the biochemical
compounds needed by the body, for exemple synthesis of proteins, enzymes,
hormones and other biocompounds which can be used in different processes.

2. In the human digestive tract, explain precisely and in details the enzymatic
catabolic processes of the following food polypeptide:

K–Y–Q–H–N–P–W–R–S–A–E–M–D–P–F
1 2 3 4 5 6 7 8 9 10 11 12 13 14

Digestion takes place in the stomach and in the small intestine.

Endopeptidases: Pepsin Chymotrypsin, Trypsin.
Pepsin: secreted by the chief cells of the stomach, activation is autocatalytic or
may be hydrolyzed by HCl. It acts as endopeptidase and has broad specificity but
prefers to cleave peptide bonds in which the amino group is provided by an
aromatic amino acid.
Chymotrypsin: secreted by the cells of the pancreas, this enzyme prefers to cleave
peptide bonds in which the carboxyl group is provided by an aromatic amino
acid.
Trypsin: secreted by the cells of the pancreas, this enzyme prefers to cleave
peptide bonds in which the carboxyl group is provided by a basic amino acid.

Exopeptidases- produced by intestinal epithelial cells act within the brush border
and also within the cell
Aminopeptidase: secreted by the cells of the small intestine, this enzyme prefers to
cleave peptide bonds in which the amino group is free (does not form any peptide
bond, it means from amino terminal end of a peptide)
Carboxypeptidase: secreted by the cells of the pancreas, this enzyme prefers to
cleave peptide bonds in which the carboxyl group is free (does not form any
peptide bond, it means from carboxylic terminal end of a peptide)

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Prolidase: secreted by the intestinal cells of the small intestine, it prefers to cleave
peptide bonds in which the secondary amino group is provided by praline (speficif
for amino group of proline)
1= pepsin 8= trypsin
2= chymotrypsin 9= Aminopeptidase
3= Aminopeptidase or carboxypeptidase 10= Aminopeptidase
4= trypsin 11= Aminopeptidase
5= prolidase 12= Aminopeptidase
6= pepsin 13= prolidase
7= chymotrypsin 14= pepsin

3. Metabolism of amino acids:

Explain the mechanism of the following reactions and (by giving at least 1
example) explain their biological importance in the functioning of the human
body: Transamination, deamination, decarboxylation.
Transamination as the name implies, refers to the transfer of an amine group
from one molecule to another. This reaction is catalyzed by a family of enzymes
called transaminases. Actually, the transamination reaction results in the
exchange of an amine group on one acid with alpha-ketone group on another
acid. It is analogous to a double replacement reaction.
The most usual and major keto acid involved with transamination reactions is
alpha - ketoglutaric acid, an intermediate in the citric acid cycle Krebs cycle). A
specific example is the transamination of Alanine to make Pyruvic acid and
glutamic acid.

Deamination is the removal of an amine group from a molecule. The enzyme

which involve in this reaction is called deaminase.
amino acid + FAD + H2O ® α-keto acid + NH3 + FADH2
During oxidative deamination, an amino acid is converted into the
corresponding keto acid by the removal of the amine functional group as
ammonia and the amine functional group is replaced by the ketone group. The
ammonia eventually goes into the urea cycle.
The keto acid is taken forward the Kreb’s cycle.
Oxidative deamination occurs primarily on glutamic acid because glutamic acid
was the end product of many Transamination reactions

Decarboxylation is a chemical reaction in which a carboxyl group (COOH) is

split off from a compound as carbon dioxide (CO2).
Enzymes that catalyze decarboxylations are called decarboxylases or, more
formally, carboxy-lyases.
For amino acids, the decarboxylation results in the synthesis of other compound
that is important physiologically such as: cysteamine, phenylethylamine, alpha
or beta-alanine, gama-butyric acid,
Amino acid – CO2 ® Amine+ CO2
Examples:
D ® alpha or beta Alanine
E ® amino butyric acid (neurotransmitter)
C® cysteamine (precursor of CoA)

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 4. Differentiate the terms essential amino acids and non-essential amino acids by
giving examples for the human beings.

5. Compare Glycogenic and ketogenic amino acids.

6. In the cases of malnutrition or under nutrition, the human body can make the
arrangements (in the term of his needs) for converting the proteins into
carbohydrates or into lipids, the carbohydrates into lipids and vice versa.
Explain precisely and in details the following conversions: (10 marks)
a) Conversion of the proteins into carbohydrates
b) Conversion of the proteins into lipids
c) Conversion of the carbohydrates into lipids
d) Conversion of carbohydrates into proteins
e) Conversion of lipids into carbohydrates

a) Conversion of the proteins into carbohydrates:

The glucogenic amino acids can undergo the deamination or transamination and
be transformed into pyruvic acid. This latter enters carboxylation and becomes
oxaloacetic acid. This latter will be transformed into phosphoenolpyruvic acid
through phosphorylant decarboxylation. The two molecules of
phosphoenolpyruvic acid enters gluconeogenesis and will become glucose.
Note: the deamination aspartic acid can produce an oxaloacetic acid which
undergoes the above mentioned way and finally produces glucose.

b) Conversion of the proteins into lipids:

The ketogenic amino acids can undergo the deamination or transamination and
be transformed into pyruvic acid. This latter enters decarboxylation in presence
of coenzyme A and becomes acetyl-coA. This latter can be used in synthesis of
fatty acids, ketone bodies, cholesterol and other compound derivate from
cholesterol.

c) Conversion of the carbohydrates into lipids:

The monosaccharide (especially glucose) undergoes glycolysis and produce

pyruvic acid. This latter enters decarboxylation in presence of coenzyme A and
becomes acetyl-coA. This later can be used in synthesis of fatty acids, ketone
bodies, cholesterol and other compound derivates from cholesterol.

d) Conversion of carbohydrates into proteins:

The monosaccharide’s (especially glucose) undergo glycolysis and produce

pyruvic acid. This later enters transamination and produces Alanine
(aminoacid). Pyruvic acid can be transformed into oxaloacetic acid by the

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 reaction of carboxylation. By transamination oxaloacetic acid becomes aspartic
acid (aminoacid).
Note: some intermediates of Krebs cycle can be used in formation of the
following amino acids:
Aspartic acid from oxaloacetic acid, glutamic acid (amino acid) from α-
ketoglutaric acid.

07. Explain the process of conversion of galactose into glucose. Explain how
Galactosemia can occur in the human body.

Galactose + ATP → galactose-1-phosphate + ADP

Galactose-1-phosphate + UDPGlc → UDPGal + Glc-1-phosphate
UDPGal → UDPGlc by UDPGal-4-epimerase
UDPGlc + PPi → Glc-1-phopsphate + UTP
Glc-1-phosphate → Glc-6-phosphate by phosphoglucomutase
Glc-6-phosphate + H2O → Glc free + Pi by Glc-6-phosphatase

The occurrence of Galactocemia in the human body: Galactosemia is a disorder

in which individuals are unable to metabolize the sugar galactose.
It is caused by deficiency of certain enzymes which include galactose-1-
phosphate uridyl transferase, UDP-galactose-4-epimerase and galactokinase.
The deficiency affects red and white blood cells and other multiple tissues
The common results of this defect are the formation of cataracts, mental
retardation, poor growth, and even death from liver damage.

08.Explain briefly the following biochemical processes and explain their

physiological importance in the functioning of the human body: aerobic cellular
respiration (= Glycolysis + Krebs cycle). Explain in details how this process
intervenes in production of energy (ATP). Explain lactic and alcoholic
fermentations.

Glycolysis: it is the process of breaking down (degradation) of monosaccharides

(mainly glucose) into 2 pyruvic acids.

These acids can be involved in different pathways depending on the needs. For
example: pyruvic acid can enter Krebs cycle if the body needs energy (ATP);
this acid can be used in synthesis of proteins by transamination or in synthesis
of lipids (this acid enters decarboxylation in presence of coenzyme A and be
transformed into acetyl-coA which will produce fatty acids or ketone bodies, all
lipids).
Krebs cycle: it is the process of synthesis of energy (ATP) from the molecules of
acetyl-coA. This energy is used by the cells in different activities, for example
during a cell division.

09. The molecules of acetyl-coA produced by β-oxidation can be used by the

human body in different ways for synthesis of bimolecular. Give at least 4 ways

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 where these molecules of acetyl-coA can be used and explain in details the
importance of these biochemical processes.

The molecules of acetyl-coA produced by β-oxidation can be used in the

following pathways:
- Synthesis of lipids (e.g new fatty acids, cholesterol, acids and salts, etc).
- Synthesis of carbohydrates and proteins (and their derivates) through
glyoxylic acid cycle
- Synthesis of ATPs through Krebs’cycle.
10. Explain briefly the triple physiological importance of cholesterol in the human
body.

Cholesterol is a waxy steroid metabolite found in the cell membrane and

transported in the blood plasma of all animals. It is an essential structural
component of mammalian cell membranes, where it is required to establish
proper membrane permeability and fluidity . In addition, cholesterol is an
important component for the manufacture of bile, acids, steroid hormones, and
several fat-soluble vitamins. Cholesterol is the principal sterol synthesized by
animals.
Cholesterol serves as a component of membranes of cells (increases or moderates
membrane fluidity), makes the cells in our body waterproof.
This is necessary because there is a different series of reactions taking place inside
and outside the cell. If there is not enough of this water insoluble alcohol in the
cell membrane cells become leaky. Nerve and muscle tissue cannot work correctly.
Cholesterol is the starting ingredient for the synthesis of the steroid hormones like
glucocorticoids (which helps in blood sugar regulation), mineral corticoids (which
helps in mineral balance and blood pressure regulation) and sex hormones
(estrogens, progesterone and testosterone). By enabling the production of bile,
which is essential for digestion, cholesterol affects all bile functions e.g., digestion
and absorption of fats and fat-soluble vitamins.

A cholesterol ester is, as its name would imply, an ester of cholesterol. The ester
bond is formed between the carboxylated group of a fatty acid and the hydroxyl
group of cholesterol. Cholesterol Esters have a lower solubility in water than
Cholesterol and are more hydrophobic. They are associated with atherosclerosis.
It helps cells in communicating with each other by transferring molecules between
them.

Cells use proteins embedded in the membrane which is facilitated by cholesterol

to communicate.
With all these benefits cholesterol is probably not that dangerous as it is made out
be but an optimum level is clearly needed for the proper functioning of the body.
A healthy diet and regular exercise help keep cholesterol at this level.

When it comes to managing optimal health and fitness, one of the most
misunderstood concepts is the role of cholesterol in the body. Hyped by the media
as a major risk factor for heart disease, cholesterol actually has a number of
important roles in the body - without which, we couldn't survive.

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While it is true that high levels of cholesterol consumed in the diet is one the top
risk factors for heart disease (the others being high blood pressure, cigarette
smoking, and diabetes), cholesterol is important for digestion, making hormones,
synthesizing vitamin D, maintaining cell membranes, learning, memory and sleep.

11. Define the term vitamin. Explain the physiological roles of the water soluble
vitamins in the human body and explain the consequences linked to the
deficiencies of those vitamins.

Vitamin is an organic compound required as a nutrient in tiny amounts by an

organism. The term vitamin was derived from "vitamine," a combination word
from vital and amine.
Today, a chemical compound is called a vitamin when it cannot be synthesized
in sufficient quantities by an organism, and must be obtained from the diet.
Vitamins are classified by their biological and chemical activity, not their
structure.

Water-soluble vitamins dissolve easily in water, and in general, are readily

excreted from the body, to the degree that urinary output is a strong predictor
of vitamin consumption.[14] Because they are not readily stored, consistent daily
intake is important.

Many types of water-soluble vitamins are synthesized by bacteria.[16] Fat-soluble

vitamins are
NAMES DEFICIENCY OVERDOSE absorbed through
OF VITAMINS DISEASES DISEASES the intestinal tract
VIT B1= Beriberi Muscle relaxation with the help of
Thiamine (chowsiness) lipids (fats). Because
they are more likely
VIT B2= Ariboflavinosis _
to accumulate in the
Riboflavin
body, they are more
VIT B3= Pellagra Liver damage likely to lead to
Niacinamide (doses) hypervitaminosis
VIT B5 Paresthesia Diarrhea, nausea, than are water-
heart burn soluble vitamins.
VIT B6 = Anemia Nerve damage.
Fat-soluble vitamin
pyridoxine
regulation is of
Pyridoxamine,
particular
pyridoxal
significance in cystic
VIT B7 dermatitis - fibrosis.
VIT B9= Folic Neural tube May mask
acid defects (birth symptoms of
defect during vitamins B12
pregnancy) deficiency other
effects. Vitamins have
VIT B12= Megaloblastic no known toxicity diverse biochemical
Cyanocobalamin anemia
VIT C = 6
scurvy Vitamin mega
Ascorbic acid dosage
 functions. Some have hormone-like functions as regulators of mineral
metabolism (e.g. vitamin D), or regulators of cell and tissue growth and
differentiation (e.g. some forms of vitamin A). Others function as antioxidants
(e.g.

Vitamin E and sometimes vitamin C)

.
The largest number ofvitamins (e.g. B complex vitamins) function as precursors
for enzyme cofactors, that help enzymes in their work as catalysts in
metabolism. In this role, vitamins may be tightly bound to enzymes as part of
prosthetic groups: for example, biotin is part of enzymes involved in making
fatty acids. Alternately, vitamins may also be less tightly bound to enzyme
catalysts as coenzymes.

12.Explain the way of synthesis and physiological importance of: gluthation

and creatin.

Creatin is an endogenous (made by the body) substance that is present in every

human cell.

Creatine is synthesized from the amino acids glycine, arginine, and methionine,

primarily in the liver, kidneys, and pancreas.It is transported from there to all
the cells in the body via the bloodstream.

It functions as an energy storehouse.

Creatin is required for physical and mental exertion and since creatine is

involved in all processes that require energy, muscle, brain and nerve cells
receive correspondingly larger amounts. The creatinereserves of a person who
weighs 70 kg equal about 120 grams. The vast majority of creatine (app. 95%)
is stored in the skeletal muscles.

Creatin is primarily involved in muscle contraction. It is taken up from the blood

into the cell membrane by means of a sodium-dependent creatine transporter.
Approximately 60-70% of the total creatine in muscle is stored in the form of the
highenergy molecule phosphocreatine. The remaining 30-40% is present in the
form of free creatine. Besides adenosine triphosphate, phosphocreatine is the most
important source for energy in the body.

All of the body’s cells can use only adenosine triphosphate (ATP) as an energy-
releasing substance. Since the ATP reserves in the body are limited, ATP has to be
continuously resynthesized. ATP is produced from the energy sources fat
and carbohydrates over a fairly long time frame. If a cell needs energy, the “high-
energy” ATP is converted to “low-energy” adenosine diphosphate (ADP). Similar
to a battery, creatine (phosphocreatine) charges low-energy ADP up to high-
energy ATP until ATP that has been converted from fat and carbohydrates is
available.

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Muscles contain 3-4 more phosphocreatine than ATP, and the phosphocreatine
serves as a short-term energy reserve for the times when the need for ATP is
greater than the synthesis of ATP from carbohydrates and fat can provide.
Phosphocreatine levels and the regeneration of ATP play key roles when the body
is involved in intense, repetitive forms of exertion.

Increasing the amount of creatine and phosphocreatine speeds up

the regeneration of ATP, which leads directly to the release and availability of
more energy.

13. Name at least 6 proteinic hormones (hormone<40 aminoacids) and explain

their physiological importance.

Antidiuretic hormone (ADH): It is produced by neurons in the hypothalamus,

transported by axons into the posterior pituitary and released from storage glands
in response to hypothalamic stimulation. Structure: it is a peptide with 9 amino
acids .Function: it stimulates water reabsorption from the filtrate in kidney, it
also plays a key role in homeostasis and the regulation of water, glucose and salt
in the blood, it raises the blood pressure; it causes contraction of involuntary plain
muscles especialy of the intestins and bladder.

Oxytocin: It is produced by neurons located in the hypothalamic Para ventricular

and supraoptic nuclei. It is a small peptide of 9amino acids .Function:-causes
uterine contraction, milk ejection in lactating females, lowers steroid synthesis in
testes, contributes to the regulation of sperm transport to the epididymis which
leads to ejaculation.

Glucagon: It is produced by alpha cells of pancreatic islets. It is a polypeptide of

29 amino acids .Function: it rises glucose level in blood by glycogenelysis
(breaking down glycogen to glucose), stimulates the hydrolysis of stored fats
(lipolysis) and consequent release of free fat into the blood which intervene
gluconeogenesis and ketogenesis.

Thyrotropin releasing hormone: also called thyrotropin releasing factor, it is

produced by hypothalamus in medial neurons of the paraverticular nucleus and is
sent to anterior pituitary lobe (gland).Structure: it is tripartite (3 amino acids)
Function: is stimulates the release of thyroid stimulating hormone and prolactin
by the anterior pituitary lobe.

Somatostatin: It is also called growth hormone –inhibiting hormone or

somatotropin release-inhibiting factor. It is secreted in digestive tract (stomach,
intestines, and delta cells of the pancreas), in neuroendocrine neurons of
periventricular nucleas of the hypothalamus in the brain) Structure: it is a
polypeptide which has two active forms, the first one has 14 amino acids and the
second has 28 amino acids.
Function:

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 -Inhibition of glucagon and somatotropin release.
-Inhibition of insulin, inhibites the release of stimulating hormone, it
suppresses the release of gastrointestinal hormone (gastrin,
cholecystokinin, secretin, motelin, vasoactive intestino peptide).

Gonadotropin releasing factor: (Gnrf, or Gnrh): it is a hormone which is

produced by hypothalamus and secreted into hypothalamic hypophyseal portal
vessels. It is also sometimes called luteinizing hormone-releasing hormone
(LHRH) Structure: it is a peptide with 10 amino acids. Function: it stimulates
anterior pituitary lobe to produce gonadotropin hormone.

15. Explain briefly how the proteins (aminoacids) can be converted into lipids
using the catabolic processes of F & Y.

F & Y are catabolized to fumarate and acetoacetate

Hydroxylation of phenylalanine to form thyrosine involves the reductant
tetrahydrobioptein like folate has a pteridine ring.

Dihydrobioptein is reduced to tetrahydroptein by electron transfer from NADH

thus thyrosine catalized by thyrosine aminotransferase enzyme is converted into
p. hydroxyphenyl pyruvate after taking in of keto glutarate and getting out of
glutamate, then p.Hydrophenyl pyuvate using p.Hydrophenylpyruvate deoxydase
and result to homogentesic acid which after being catalised by homogentesic
deoxygenase enzyme result to mallyl acetoacetate.

Then mallylacetoacetate is catalised by mallylacetoacetate isomerase and gives

fumaryllacetate which result to the acetoacetate + fumarate after fumarylacetate
reaction.

16. Explain in details how the following metabolic diseases can occur in the
human body: Phenylketonuria, Alcaptonuria, and Scorbut using the catabolic
processes of F & Y.

Phenylketonuria: it is an autosomal recessive genetic disorder characterized by a

deficiency in the hepatic enzyme phenylalanine hydroxylase (PAH).

This enzyme is necessary to metabolize the amino acid phenylalanine to the amino
acid tyrosine. When phenylalanine hydroxylase is deficient, phenylalanine
accumulates in the blood and is converted into phenylpyruvate (phenylketones)
via a transaminase path way which is detected in the urine.

It can cause problems with brain development leading to progressive mental

retardation, brain damage and seizure.
The enzyme phenylalanine hydroxylase normally converts the amino acid
phenylanine into amino acid tyrosine if this reaction doesn’t take place,
phenylanine accumulates and tyrosine is deficient.

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 .

Alcaptonuria: It is a genetic
• Phenylalanine Transaminasephenylpyruvate
disorder of phenylalanine
Phenylalanine
Phenylalanine
hydroxylase
hydroxylase absent and tyrosine metabolism. It
present
is characterized by lack of
Tyrosine
the enzyme homogentisate
Melanins
1, 2-dioxygenase which
metabolizes phenylalanine
Fumarate+Acetoacetate and tyrosine. These amino
acids accumulate in the
blood leading to excretion of homogentisic acid (alkapton) in the urine.
Urine turns black if it is allowed to stand.

Scorbut: It is a metabolic disorder which results from a deficiency or inactivation

of para-hydro-phenyl-pyruvate oxydase enzyme.

This enzyme metabolises phenylalanine and tyrosine. It is characterised by

elimination of para-hydroxy-phenyl–pyruvic acid and para-hydroxy-phenyl
lactic acid in the urine.

17. In the human digestive tract, explain precisely and in details the enzymatic
catabolic processes of the following food carbohydrates: sucrose, lactose, maltose,
trehalose, starch, glycogen, cellulose.

Sucrose: it is readily digested in the stomach into its components sugar, by acidic
hydrolysis, glucose and fructose are rapidly absorbed into the blood stream in the
small intestine.

Undigested sucrose passing into intestine is also broken down by sucrase or

glucosidic hydrolysis which are located in the membrane of microvilii living in
duodenum.
Sucrose is digested by the enzyme invertase (also called sucrase or beta
fructosidase).
Lactose: it is composed by glucose and galactose and it is found in the milk. This
monosaccharides are linked together by beta 1-4 galactosidic bond. The enzyme
which breaks down this bond is Beta galactosidase (or lactase).

Maltose (malt sugar): it is composed by 2 glucose units linked by alpha 1-4

glucosidic bond. Maltose is formed intermediately in digestive tract during
breaking down the polysaccharides (starch, glycogen), that bond is broken down
by maltase.

Trehalose is composed by 2 molecules of glucose linked together by alpha 1-1

glucosidic bond and this sugar is found in fungi. In digestive tract this bond in
trehalose is broken down by the enzyme called trehalase.

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Starch is composed of many molecules of glucose linked together by alpha 1-4
glucosidic bonds. It is synthesized only by the plant cells.
There are 2 forms of starch:
- Amylose: In which molecules of glucose are linked together
in straight chains. It has hydrogen bonds but not ramifications.
- Amylopectine: In which the glucose chains are highly
branched. Each lateral chain composed of alpha 1-4 osidic bonds of glucose and
alpha 1-6 osidic bonds link lateral chains with main chains.
The following enzymes are involved in degradation of starch:

Alpha amylase will break down alpha 1-4 glucosidic bonds in main and lateral
chains forming the molecules of maltose and residual dextrines.
-Amylo alpha 1-6 glucosidase will break down alpha 1-6 glucosidic bonds.
Maltase will break down alpha 1-4 glucosidic bond in maltose.
Glycogen is a polysaccharide synthesized in liver and muscles. It is formed by
large polymers of glucose and is the major animal storage carbohydrate it has
structure as the same amylopectin of starch.

The enzymes which help in glycogen are: Alpha Amylase break down Alpha 1-4
glucosidic bonds.
Amylo Alpha 1-6 glucosidase break down Alpha1-6 osidic bonds
Maltase is ready to break down Maltose includes 2 molecules of glucose.

Cellulose: Is carbohydrate which synthesized by the plant cells. It is composed by

linear chains of D- glucose molecules linked to one other by beta 1-4 glucosidic
bonds. These bonds are broken down by enzyme called cellulose which is never
synthesized by the human body.

18. Explain briefly the following biochemical processes and explain their
physiological importance in the functioning of the human body: Glycogenesis &
Pentose-Phosphate Pathway (for PPPW explain at least triple role).

Glycogenesis: it is the process of glycogen synthesis from glucose. In this process

glucose molecules are added to chains of glycogen. It helps in temporary storage
of glucose molecules which are not immediately needed by the body cells from
meal.

Pentose-Phosphate Pathway:

The interests of this pathway are:

- It provides pentose-phosphates which are essential for the synthesis of
nucleotides that are found in various coenzymes (examples: FAD, NAD, NADP)
and in nucleic acids (examples: DNA, RNA).

It leads to the formation of NADPH for various important reactions:

- During the biosynthesis of fatty acids, the synthesis of sterols.
- Reducing tetrahydrofolic acid into dihydrofolic acid. During the process
ofcarboxylation of pyruvic and malic acids.

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 - When these reactions do not occur, the NADPH can lead to the formation of
energy by the NAD transhydrogenation committed then, under its reduced form
NADH in the chain of oxidative phosphorylation. (Examples: ATP

19.In the functioning of the human body, explain in details the role of the
following lipidic compounds: prostaglandins, leucotrienes, PAF acether,
cerebrosides, sulfatides.

Prostaglandin is any member of a group of lipid compounds that are derived

enzymatically from fatty acids and have important functions in the human body.

The diversity of receptors means that prostaglandins act on an array of cells and
have a wide variety of effects such as: cause constriction or dilation in vascular
smooth muscle cells, cause aggregation or disaggregation of platelets, sensitize
spinal neurons to pain, decrease intraocular pressure, regulate inflammatory
mediation, regulate calcium movement, control hormone regulation, control cell
growth, act on thermoregulatory center of hypothalamus to produce fever.
Leukotrienes are fatty molecules of the immune system that contribute to
inflammation in asthma and bronchitis.

Leukotrienes are involved in asthmatic and allergic reactions and act to

sustain inflammatory reactions.
Several leukotriene receptor antagonists such as montelukast and zafirlukast
are used to treat asthma.
Leukotrienes are very important agents in the inflammatory response.

Leukotrienes also have a powerful effect in bronchoconstriction and increase

vascular permeability.

Leukotrienes assist in the pathophysiology of asthma, causing or potentiating

the following symptoms:
Airflow obstruction, increased secretion of mucus, mucosal accumulation,
bronchoconstriction,
Infiltration of inflammatory cells in the airway wall.
PAF-acether (Platelet-activating factor, also known as a PAF, or AGEPC
(acetyl-glyceryl-ether-phosphorylcholine) is a potent phospholipids activator
and mediator of many leukocyte functions, including platelet aggregation,
inflammation and anaphylaxis. It is an important mediator of
bronchoconstriction.

It causes platelets to aggregate and blood vessels to dilate. Thus it is

important to the process of hemostasis

Cerebrosides are the common name for a group of glycosphingolipids called

monoglycosylceramides which are important components in animal muscle
and nerve cell membranes. It is essential for lamellar body formation in the

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 stratum corneum. Maintain the water permeability barrier of the skin. A
defect in degradation of glucocerebrosides in Gaucher's disease..The
corresponding defect for galactocerebrosides is Krabbe disease.

Sulfatides are a class of sulfated galactosylceramides synthesized primarily

in the oligodendrocytes in the central nervous system. Sulfatides are a type
of sulfolipid.
Play an important role in myelin function with galactocerebrosides and
stability.
Powerful function in coagulation system, activate blood coagulation factor xii.
Has a physiological function in cells adhesion.
Act as coagulant and anticoagulant in the blood.

20. Explain the physiological roles of the fatty soluble vitamins in the human body
and explain the consequences linked to the deficiencies of those vitamins. Define
the term avitaminosis.

Vitamin A: Helps to form skin and mucous membranes and keep them healthy,
thus increasing resistance to infections; essential for night vision; promotes bones
and tooth development. Beta carotene is an antioxidant and may protect against
cancer.

Vitamin D: Promotes hardening of bones and teeth, increases the absorption of

calcium. Helps to make calcium and phosphorus available in the blood. The body
can synthesize it with the help of sunlight.

Vitamin E: Vitamin E is a fat-soluble antioxidant. It protects other substances

from oxidation by being oxidized itself e.g. vitamin A and C therefore naturally
occurring tocopherols.Tocopherol ( 5, 7,8 trim ethyl tocol) is the most active and
abundant one. Vitamin E as an antioxidant prevents damage to cell membranes.
Antioxidant

Vitamin K: Blood clotting. At least 13 different proteins and the mineral Ca2+are
involved in making blood clotting.
Vitamin K is essential for the activation of one of these proteins, among of them
prothrombin, the precursor of thrombin. When any of the blood-clotting factor is
lacking hemorrhage disease occurs. Helps blood to clot.

Explain briefly the process of β-oxidation of fatty acids. Explain the completely
oxidation of fatty acids and its physiological importance.
β-oxidation is the process by which fatty acids, in the form of Acyl-CoA
molecules, are broken down in mitochondria and/or in peroxisomes to generate
Acetyl-CoA, the entry molecule for the Krebs cycle.

The molecules that start this cycle (the inputs) are the saturated fatty acid and
coenzyme A products (fatty acyl-CoA). The fatty acids involved can be even
numbered carbon chains with no double bonds.  Some other inputs that are added

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after the cycle has started are FAD (flavine adenine dinucleotide), water, ATP,
and NAD+(nicotinamide adenine dinucleotide).

The products of this pathway (the outputs) include FADH2, NADH, acetyl-CoA,
and of course, the final products.  The final fatty acid products are acetyl-CoA for
the even numbered fatty acids (without double bonds), and for those with an odd
number of carbons, it is 3-carbon propionyl-CoA instead.
The beta oxidation of fatty acids involves three stages:
Activation of fatty acids in the cytosol
Transport of fatty acids into mitochondria
Beta oxidation proper in the mitochondrial matrix

Activation of fatty acids

Free fatty acids can penetrate the plasma membrane due to their poor water
solubility and high fat solubility. Once in the cytosol, a fatty acid reacts with ATP
to give a fatty acyl adenylate, plus inorganic pyrophosphate. This reactive acyl
adenylate then reacts with free coenzyme A to give a fatty acyl-CoA ester plus
AMP (adenosine monophosphate).

1. Dehydrogenation by FAD: The first step is the oxidation of the fatty acid by
Acyl-CoA-Dehydrogenase. The enzyme catalyzes the formation of a double bond
between the C-2 and C-3.

2. Hydration: The next step is the hydration of the bond between C-2 and C-3
3. Oxidation by NAD+: The third step is the oxidation of L-β-hydroxy acyl CoA by
NAD+. This converts the hydroxyl group into a keto group.

4. Thiolysis: The final step is the cleavage of β-keto acyl CoA by the thiol group of
another molecule of CoA. The thiol is inserted between C-2 and C-3.

i. 21.The human body completely oxidizes the stearic acid and a molecule of
galactose to produce the maximum amount of energy ATP needed in various
cellular activities: Explain and show how the lipids produce more energy than
carbohydrates by calculating the energy yield (rendement énergétique) per
carbon atom for lipids and for carbohydrates.

i.First of all, the galactose must be converted into glucose to be metabolized.

Glucose enters into glycolysis and produces 2 molecules of pyruvic acid and 8
molecules of ATP. These molecules of pyruvic acid will enter the Krebs cycle
and generate 12 × 2 = 24 ATP. The total number of ATP produced by complete
oxidation of one molecule of galactose (C6) = 38ATP

ii. Stearic acid is first activated and turns into stearyl-CoA in the presence of one
molecule of ATP). The stearyl-CoA enters a process of β-oxidation and each
round of β-oxidation produces an acetyl-CoA and a new acyl-CoA with 2 carbon
atoms less. This acyl-CoA between enters in new the β-oxidation and so on until
all the stearyl-CoA becomes totally 9 molecules of acetyl-CoA with 8 β-oxidation.

14
 Each round of β-oxidation produces 5 ATP (5 × 8 = 40ATP). Each acetyl-CoA
produces 12ATP in the Krebs cycle (12 × 9 = 108ATP). The total number of ATP
= ((40ATP + 108ATP) - 1ATP) = 147ATP/18carbone of stearic acid.

iii. The energy efficiency through carbon atom in the carbohydrate: 38ATP = 6.33
ATP/1 carbon
                                                                                                           6
 iv. The energy efficiency through carbon atom in the lipid: 147ATP = 8.16 ATP/1
carbon

18  
By comparing yields énergétique, we see that the lipids that are more énerégtiques
carbohydrates (8.16 ATP / 1 carbon lipid and 6.33 ATP / 1 carbon from
carbohydrates).
                                                                                                            
                                                                                                            

Explain 3 ways of occurring of albinism in the human body.

13.Human tyrosinase is a single membrane spanning transmembrane
protein In humans, tyrosinase is sorted into melanosomes and the
catalytically active domain of the protein resides within melanosomes.
Only a small enzymatically non-essential part of the protein extends into
the cytoplasm of the melanocyte.
14.Albinism (from Latin albus, "white"; see extended etymology, also called
achromia, achromasia, or achromatosis) is a congenital disorder
characterized by the complete or partial absence of pigment in the skin,
hair and eyes due to absence or defect of an enzyme involved in the
production of melanin. Albinism results from inheritance of recessive
gene alleles and is known to affect all vertebrates, including humans. The
most common term used for an organism affected by albinism is
"albino". Additional clinical adjectives sometimes used to refer to
animals are "albinoid" and "albinic".
15.Albinism is associated with a number of vision defects, such as
photophobia, nystagmus and astigmatism. Lack of skin pigmentation
makes the organism more susceptible to sunburn and skin cancers.
16.Most forms of albinism are the result of the biological inheritance of
genetically recessive alleles (genes) passed from both parents of an
individual, though some rare forms are inherited from only one parent.
There are other genetic mutations which are proven to be associated with
albinism. All alterations, however, lead to changes in melanin production
in the body.
17.The chance of offspring with albinism resulting from the pairing of an
organism with albinism and one without albinism is low. However,
because organisms can be carriers of genes for albinism without
exhibiting any traits, albinistic offspring can be produced by two non-
albinistic parents. Albinism usually occurs with equal frequency in both
genders An exception to this is ocular albinism, which it is passed on to
offspring through X-linked inheritance. Thus, ocular albinism occurs
more frequently in males as they do not have a second X chromosome

15
 18.There are two of different forms of albinism; a partial lack of the melanin
is known as hypomelanism, or hypomelanosis and the total absence of
melanin is known as amelanism or amelanosis.
19.Genetic mutations that affect the production of a pigment called melanin.
There is a cell called the melanocyte that is responsible for giving skin,
hair, and eyes pigmentation. In albinism, the melanocytes are present, but
genetic mutations interfere with their pigment production or their ability
to distribute it to keratinocytes, the major cell type comprising the
epidermis, or outer layer of the skin.
20.Albinism was formerly categorized as tyrosinase-positive or -negative. In
cases of tyrosinase-positive albinism, the enzyme tyrosinase is present.
The melanocytes (pigment cells) are unable to produce melanin for any
one of a variety of reasons that do not directly involve the tyrosinase
enzyme. In tyrosinase-negative cases, either the tyrosinase enzyme is not
produced or a nonfunctional version is produced. This classification has
been rendered obsolete by recent research
21.

22.Explain how G & Q are involved in the processes of detoxication of the

human body and explain the role of G in synthesis of Hb (heme).
Detoxification : is the process of making harmfull substances(toxins) into
harmless substances. In the body it occurs mainly in the liver. It occurs in two
phases:
When amino acids are deaminated releases ammonia which is toxic for nervous
cells. then our body stores this ammonia as glutamine which is not toxic for our
body.
glutamine releases ammonia as urea in the liver and in the kidney as
ammonium ion.
Glycine serves as an effective conjugative detoxicans.
Salicyclic acids and nicotinic acid are similarity detoxicified by conjugation with
glycine.
Glycine can react with benzoic acid (toxic acid) and the product is hippuric acid
which is not roxic.
Glutamine can react with phenyl acetic acid (toxic) and produces phenyl acetyl
glutamine which is less toxic that phenyl acetic acid. This phenyl acetic acid
comes from phenyl lactic acid, this later is the result of deamination of
phenylalanine during phenylketonuria.
the role of G in synthesis of Hb (heme).
Heme is the prosthetic group of hemoglobin, myoglobin, and the cytochromes.
Heme synthesis begins with condensation of glycine & succinyl-CoA, with
decarboxylation, to form d-aminolevulinic acid (ALA) by ALA synthase.
PBG Synthase (Porphobilinogen Synthase), also called ALA Dehydratase,
catalyzes condensation of two molecules of d-aminolevulinic acid (ALA) to form
porphobilinogen (PBG).
 Uroporphyrinogen III Synthase converts the linear tetrapyrrole
hydroxymethylbilane to the macrocyclic uroporphyrinogen III.
Conversion of uroporphyrinogen III to protoporphyrin IX (above) occurs in
several steps, as presented in the animation below:

16
decarboxylation of all 4 acetyl side chains, converting them to methyl groups
(catalyzed by Uroporphyrinogen Decarboxylase).
oxidative decarboxylation of 2 of the 4 propionyl side chains, converting them to
vinyl groups (catalyzed by Coproporphyrinogen Oxidase)
oxidation adds more double bonds (catalyzed by Protoporphyrinogen Oxidase),
yielding protoporphyrin IX.
Fe++ is added to protoporphyrin IX via Ferrochelatase. This enzyme in
mammals is homodimeric and contains two [2Fe-2S] iron-sulfur clusters. A
conserved active site histidine, along with a chain of anionic residues, may
conduct released protons away, as Fe++ binds from the other side of the
porphyrin ring, to yield heme.

23.Explain precisely and in details the triple physiological importance of Y

in the human body.
24.Detoxification : is the process of making harmfull substances(toxins) into
harmless substances. In the body it occurs mainly in the liver. It occurs in
two phases:
25.When amino acids are deaminated releases ammonia which is toxic for
nervous cells. then our body stores this ammonia as glutamine which is
not toxic for our body.
26.glutamine releases ammonia as urea in the liver and in the kidney as
ammonium ion.
27.Glycine serves as an effective conjugative detoxicans.
28.Salicyclic acids and nicotinic acid are similarity detoxicified by
conjugation with glycine.
29.Glycine can react with benzoic acid (toxic acid) and the product is
hippuric acid which is not roxic.
30.Glutamine can react with phenyl acetic acid (toxic) and produces phenyl
acetyl glutamine which is less toxic that phenyl acetic acid. This phenyl
acetic acid comes from phenyl lactic acid, this later is the result of
deamination of phenylalanine during phenylketonuria.
31. the role of G in synthesis of Hb (heme).
32.Heme is the prosthetic group of hemoglobin, myoglobin, and the
cytochromes.
33.Heme synthesis begins with condensation of glycine & succinyl-CoA, with
decarboxylation, to form d-aminolevulinic acid (ALA) by ALA synthase.
34.PBG Synthase (Porphobilinogen Synthase), also called ALA Dehydratase,
catalyzes condensation of two molecules of d-aminolevulinic acid (ALA)
to form porphobilinogen (PBG).
35. Uroporphyrinogen III Synthase converts the linear tetrapyrrole
hydroxymethylbilane to the macrocyclic uroporphyrinogen III.
36.Conversion of uroporphyrinogen III to protoporphyrin IX (above) occurs
in several steps, as presented in the animation below:
37.decarboxylation of all 4 acetyl side chains, converting them to methyl
groups (catalyzed by Uroporphyrinogen Decarboxylase).
38.oxidative decarboxylation of 2 of the 4 propionyl side chains, converting
them to vinyl groups (catalyzed by Coproporphyrinogen Oxidase)

17
 39.oxidation adds more double bonds (catalyzed by Protoporphyrinogen
Oxidase), yielding protoporphyrin IX.
40.Fe++ is added to protoporphyrin IX via Ferrochelatase. This enzyme in
mammals is homodimeric and contains two [2Fe-2S] iron-sulfur clusters.
A conserved active site histidine, along with a chain of anionic residues,
may conduct released protons away, as Fe++ binds from the other side of
the porphyrin ring, to yield heme.

41.Explain briefly the following biochemical processes and explain their

physiological importance in the functioning of the human body:
Glyconeogenesis & Glycogenolysis.

42.Explain briefly the process of β-oxidation of saturated fatty acids. Explain

the role of Krebs cycle in the oxidation of fatty acids and explain the
completely oxidation of these two fatty acids.

43.Explain in details the process of ketogenesis and explain its physiological

importance.
44.Explain precisely how acetoacetic acid can be used by some organs to
produce the energy ATP.

45.Explain and compare the structures of nucleic acids (DNA, mRNA, rRNA,
tRNA) and explain their main functions in the functioning of the human
body.

46.In the cases of malnutrition or undernutrition, the human body can make
the arrangements (in the term of his needs) for converting the proteins
into carbohydrates or into lipids, the carbohydrates into lipids and vice
versa. Explain precisely the process of conversion of lipids into
carbohydrates and proteins using the glyoxylate cycle.

47.The human cell completely oxidizes one molecule of 9-methyl

heptadecanoïc acid to produce energy (ATPs) needed in various cellular
activities: explain how this acid is completely oxidized and how those
energetic molecules are synthesized by writing precisely the main steps
on which ATPs are produced and by indicating the total number of ATP
produced on each step. Finally, calculate the total number of ATPs gained
by the cell.

48. Detoxification of the human body: explain how ammonia (product of

deamination of amino acids ) is transformed into urea cycle (one ways of
elimination of toxic ammonia).

49. Match the following:

18
 1. Albinism A.Is a hypoglycemic process
decreasing the level of glucose in
blood
2. Glycogenolysis B.Is a metabolic disorder caused
by the deficiency of
homogentisate oxydase in the
body
3. Oxytocin C. Is a metabolic disorder caused
by the deficiency of tyrosinase in
the body
4. Glucagon D.Is a metabolic process increasing
the level of glucose in blood
5. Glycogenesis E. Participates in digestion of
dietary polymers in the human
gastrointestinal tract
6. PPPW F. causes the uterine contraction
and milk ejection in lactating
females
7. Taurochalate of G.Increases the glucose level in
sodium blood by stimulating
glycogenolysis
8. Alcaptonuria H.stimulates water reabsorption
from the filtrate in kidney
9. Glutamine I. produces the molecules of
pentose-phosphates which are
essential for the synthesis of
nucleotides and nucleic acids
10. Antidiuretic J. Is one of the amino acids which
hormone participate in the process of
detoxication of thenhuman body
by neutralizing the toxic
compounds

50. Complete the following biochemical reactions by filling in the blanks

accordingly. (10 marks)

a. Alanine + αketoglutarate............Transamination
pyruvate......................... + Glutamate
b. Aspartate Deamination ......................ammonia.......+ acetoacetic
acid................................
c. Serine Decarboxylation ethanamine.......................... + CO2
d. glutamine ........................ Decarboxylation γ-aminobutyrate + CO2

19
 e. Glycogen(n residues) + pi............ glycogenolysis glycogen (n–1 residues) + .glucose-1-
phosphate.................
f. Glucose-6-phosphate the complete oxidative phase of PPPW ribulose-5-
phosphate ..............+ ..NADH.......... + CO2

51. Fill in the blanks:

A.The biochemical process facilitating the temporally storage of the dietary

monosaccharides not immediately used by the body is …
glucogenesis…………………………………………………

B. The main biochemical processes by which fatty acids are completely oxidized
and transformed into carbon dioxide and water by producing energy are …β-
oxidation............................…………
C. ketogenesis……………. is the biochemical process by which ketonies bodies are
synthesized in the liver.

D.translation……………..is the process of the transfer of genetic information from

mRNA to rRNA

E. The biochemical process by which the molecules of acetyl-CoA which are not
immediately used by the human body are stored is ketogenesis……………….
……………………….

F. glucolysis……………………. is the extramitochondrial process by which energy is

synthesized.

G.galactosemia…………………. is a congenital metabolic disorder caused by the

deficiency of the enzyme “phosphogalactose uridyl transferase”.

H.The process of the transfer of genetic information from DNA to mRNA is called
transcription…………

52.1. Metabolism of monosaccharides: in the human body the metabolism of the

dietary galactose always starts by its conversion into glucose. This conversion
occurs through a series of steps. Explain in detail the mechanism of the
enzymatic conversion of galactose into glucose by indicating all the enzymes
involved in that process.

53.Describe briefly the following biochemical processes and explain their

physiological importance in the functioning of the human body:
a) Glycogenolysis
b) Glycogenesis
c) Glyconeogenesis
d) β-oxidation
e) Cellular aerobic respiration
…………………………………………………………………………………………………

20
 Multiple choice questions

1. The monomers for the nucleic acids are called_________

a. Nitrogenous bases
b. Sugars
c. Pentose-phosphate group
d. Nucleotides

2. Which of the following statements is TRUE for RNA molecule?

a. Most RNA usually occurs in the cytoplasm while a very little RNA is found
inside nucleus
b. RNA is usually double stranded with a unique polynucleotidic chain
c. RNA contains the genetic information
d. Purine and Pyrimidine bases in RNA are in equal number

3. The two polynucleotidic chains of DNA are linked together by:

a. Covalent bond
b. Hydrogen bonds
c. Phosphodiester bond
d. Ionic bond

4. Inside a nucleic acid the nucleotides are joined by _______

a. 1’- 4’ phosphodiester bonds
b. 5’- 1’ phosphodiester bonds
c. 3’- 5’ phosphodiester bonds
d. 1’- 6’ phosphodiester bonds
5. The term “metabolism” refers to _______
a. the digestion of the food polymers into monomers
b. the synthesis of big molecules from simpler molecules.
c. the breakdown of big molecules into small molecules.
d. the anabolic and catabolic processes.

6. Nutritional polysaccharides are ______

a. starch and glycogen
b. starch and chitin
c. starch and cellulose
d. starch and glucose

7. In the human body the glycogen molecules are mainly stored in _______
a. liver and muscles
b. liver and pancreas
c. Muscles and bile

21
 d. liver and adipose tissue

8. The association between the sugars and proteins makes _______

a. glycolipids
b. glycoproteins
c. galactosides
d. ganglioside

9. The intracellular complete oxidation of a molecule of fatty acid involves the

following stepts in order______
a. Glycolysis, β-oxidation, Krebs cycle, Electron transport system
b. β-oxidation, Krebs cycle, Electron transport system
c. β-oxidation, Glycolysis, Krebs cycle, Electron transport system
d. β-oxidation, Krebs cycle, Glycolysis, Electron transport system

10. A living cell involves a C26 saturated fatty acid in β-oxidation for getting an
amount of ATPs to use in different cell activities: how many rounds of β-
oxidation are needed to convert C26 saturated fatty acid into the molecules of
acetyl-CoA and how many molecules of acetyl-CoA are produced?
a. 13 rounds and 12 acetyl-CoA
b. 11 rounds and 12 acetyl-CoA
c. 12 rounds and 13 acetyl-CoA
d. None of the above

11. A living cell involves a C26 saturated fatty acid in the complete oxidation
(β-oxidation, Krebs cycle and electron transport system) for getting an
amount of ATPs to use in different cell activities: how many ATPs are
produced?
a. 60
b. 156
c. 216
d. 204

12. In the human digestive tract the food glycogen is digested respectively by
the following enzymes:
a. Lactase, α-amylase, amylo-α-1,6 glycosidase, maltase
b. α-amylase, maltase, amylo-α-1,4 glycosidase, ,
c. Lactase, invertase, α-amylase, amylo-α-1,6 glycosidase, maltase
d. α-amylase, amylo-α-1,6 glycosidase, maltase
13. The term “metabolism” refers to _______
a. the digestion of the food polymers into monomers
b. the anabolic and catabolic processes
c. the synthesis of big molecules from simpler molecules.
22
 d. the breakdown of big molecules into small molecules.

14. The highly branched polymer of glucose molecules is ______________

a. Cellulose
b. Starch
c. Glycogen
d. amylose

15. All the following enzymes participate in digestion of dietary polymers in

the digestive tract, except:
a. Pepsin
b. alpha-amylase
c. Invertase
d. Decarboxylase
16. Nutritional polysaccharides for the human beings are ______
a. starch and glycogen
b. starch and chitin
c. Glycogen and cellulose
d. None of the above
17. In the human muscle cells the process of anaerobic glycolysis is always
followed by_____________
a. Alcoholic fermentation
b. Lactic fermentation
c. Krebs cycle
d. Glycogenesis

18. In the human body the essential aminocids are always provided by
____________
a. Transamination
b. Glucogenic aminoacids
c. Taken food
d. None of the above

19. Which of the following biochemical process is NOT hypoglycemic?

a. Glycolysis
b. Pentose phosphate pathway
c. Glycogenesis
d. Glycogenolysis

20. Glucogenic aminoacids are_______________

a. aminoacids that can be used to convert the proteins to lipids

23
 b. aminoacids that can be used to convert the proteins to carbohydrates
c. aminoacids that can be converted to glycolysis
d. Both A and B are correct

21. In the human body the glycogen molecules are mainly stored in _______
a. liver and pancreas
b. Muscles and bile
c. liver and muscles
d. liver and adipose tissue
22. The main function of Hb in the human body is ___________
a. to carry O2 molecules from the lungs to the tissue cells
b. to carry CO2 molecules from the tissue cells to the lungs
c. to carry blood from the heart to the tissue cells and lungs
d. Both A and B are correct

23. The organs involved in order in the catabolic process of Hb provided by

the dead RBC are_______
a. spleen, liver, small intestine
b. bilirubin, glucuronic acid, stercobilinogen
c. blood, liver, kidney
d. Both A and B are correct

24. Which of the following compunds is involved in the catabolism of Hb in he

human body?
a. Ribose
b. Glucuronic acid
c. Inositol
d. Gluconic acid

25. Which of the following biochemical processes is NOT hyperglycemic?

a. Glyconeogenesis
b. Glycogenolysis
c. Glycogenesis
d. Both B and C are correct

26. In microorganisms the process of anaerobic glycolysis is followed

by_____________
a. Lactic fermentation
b. Krebs cycle

24
 c. Glycogenesis
d. Alcoholic fermentation

27. Metabolism of aminoacids: decarboxylation reactions can be used by the

living cells to _______
a. breakdown the food proteins to monomers
b. synthesize the non-essential amino acids
c. synthesize the needed energy
d. Both B and C are correct

28. In the human digestive tract the food glycogen is digested respectively by
the following enzymes:
a. Lactase, α-amylase, amylo-α-1,6 glycosidase, maltase
b. α-amylase, maltase, amylo-α-1,4 glycosidase, ,
c. α-amylase, amylo-α-1,6 glycosidase, maltase
d. Lactase, invertase, α-amylase, amylo-α-1,6 glycosidase, maltase

29. Metabolism of aminoacids: α-ketoglutarate is a predominant amino-

acceptor in the transamination reactions where it replaces its ketone group
by amino group and becomes:
a. α-ketoacid
b. Aspartate
c. γ-aminobutyrate
d. Non essential amino acid

30. The dephosphorylation of Glc-6-P in the liver functions to allow the

glucose molecules _______
a. to leave the liver and be transported to different sites of the body
b. to enter different pathways inside the hepatocytes
c. to be used in glycogenolysis
d. None of the above

31. In the adult humans one molecule of Hb contains normally __________

a. 2 α chains and 2 γ chains
b. 2 α chains and 2 β chains
c. 2 β chains and 2 γ chains
d. None of the above

32. The association between the sugars and proteins makes _______
a. glycolipids
b. galactosides
c. glycoproteins
25
 d. ganglioside
33. Which of the following is a steroid hormone stimulating the process of
spermatogenesis?
a. Testosterone
b. Aldosterone
c. Progesterone
d. Cortisone

34. Which of the following is a nucleic acid involved in the transfer of genetic
information from the nucleus to the cytoplasm of an eukaryotic cell?
a. DNA
b. RNAm
c. RNAr
d. RNAt

35. It is a water soluble vitamin that plays an important role in the process of
RBC growth _____
a. Vitamin B6
b. Vitamin D
c. Vitamin B12
d. Vitamin K

36. Which of the following fatty acids is essential for the human beings_______
a. Oleic acid
b. Palmitic acid
c. Butyric acid
d. Linoleic acid

37. The process of transfer of the genetic information from DNA to RNA m is
called_________
a. Transcription
b. Translation
c. RNA polymerase
d. DNA synthetase

38. Translation is a process of transferring the genetic information from

RNAm to RNAt is called_________
a. RNAm to RNAt
b. RNAt to RNAr
c. RNAm to RNAr
d. DNA to RNAm

26
39. Which of the following is the final product of the degradation of Hb in the
spleen?
a. Globin
b. Bilirubin
c. Stercobilin
d. Urobilin

40. Which of the following is NOT a ketone body?

a. Acetoacetate
b. Acetyl-CoA
c. Acetone
d. Β-hydroxybuturate

41. Which of the following is a lipidic compound synthesized by the blood

platelets and participating in the process of blood clotting?
a. Glycolipide
b. Fatty acid
c. PAF acether
d. Ketone body

42. It is a lipidic compound that acts as the myelin sheath in the nervous
system:
a. Prostaglandin
b. Glyceride
c. Cerebroside
d. Leukotriene

43. Which of the following statements is NOT TRUE for a DNA molecule?
a. DNA usually occurs inside nucleus and some cell organelles
b. DNA contains the genetic information
c. Purine and Pyrimidine bases of DNA are in equal number
d. DNA is usually single stranded with two polynucleotidic chains
44. The equation C6H12O6+6O6 6CO2+6H2O+energy (ATP) refers to
_______
a. β-oxidation, glycolysis, Krebs cycle and electron transport system
b. Aerobic glycolysis, Pentose phosphate pathway and Krebs cycle
c. β-oxidation, Krebs cycle, glycolysis, electron transport system
d. Cellular aerobic respiration

27
45. The organs involved (in order) in the degradation of Hb provided by the
dead RBC are_______
a. spleen, liver, small intestine
b. bilirubin, glucuronic acid, stercobilinogen
c.blood, liver, kidney
d. Both B and C are correct

46. In the adult humans one molecule of Hb contains normally __________

a. 2 α chains and 2 γ chains
b. 2 α chains and 2 β chains
c. 2 β chains and 2 γ chains
d. None of the above

47. Which of the following chains is complementary to this DNA chain ....A-G-
C-T-A-T-C-G....?
a. A-G-C-A-T-A-C-C
b. T-C-C-T-A-T-G-C
c. T-C-G-A-T-A-G-C
d. A-C-G-A-T-A-G-G

48. Metabolism of aminoacids: α-ketoglutarate is a predominant amino-

acceptor in the transamination reactions where it replaces its ketone group by
amino group and becomes:
e. essential amino acid
f. α-ketoacid
g. Aspartate
h. glutamate

49. Metabolism of aminoacids: decarboxylation reactions can be used by the

living cells to _______
e. synthesize the non-essential amino acids
f. breakdown the food proteins into monomers
g. synthesize the needed energy
h. Both B and C are correct

50. The dephosphorylation of Glc-6-P in the liver functions to allow the

glucose molecules _______
e. to leave the liver and be transported to different sites of the body
f. to enter different pathways inside the hepatocytes
g. to be used in glycogenolysis
h. None of the above

28
51. The urea (the end product of urea cycle) is routinely measured in the
blood as ________
a. Urea cycle nitrogen
b. Blood urea nitrogen
c. Uric acid nitrogen
d. Blood Ammoniac acid

52. The process in which the genetic information is transferred from DNA to
RNA is called ______
a. replication
b. transcription
c. translocation
d. translation

53. The process in which the genetic information is transferred from RNA m to
RNAr is called _____
a. replication
b. translocation
c. translation
d. transcription

54. Which of the following biochemical processes is NOT hypoglycemic?

a. Glycolysis
b. Pentose phosphate pathway
c. Glycogenolysis
d. Glycogenesis

55. The main function of Hb in the human body is ___________

e. to carry O2 molecules from the lungs to the tissue cells
f. to carry CO2 molecules from the tissue cells to the lungs
g. to carry blood from the heart to the tissue cells and lungs
h. Both A and B are correct

56. Which of the following biocompunds is involved in the catabolism of Hb

in the human body?
a. Bilirubin
b. Triglyceride
c. Amino acid
d. Glucuronic acid

29
57. Match the following fatty soluble vitamins with their functions in the
human body:

Vitamin Function
1. Vitamin A A. Prevention of
2. Vitamin K oxidative damage
3. Vitamin E B. Calcium and
4. Vitamin D phosphate metabolism
C. Vision
D. Blood clotting

30