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ASSIGNMENT
Subject: CLINICAL BIO CHEMISTRY
ANSWERS
1. Carbohydrates cannot be hydrolysed into a simpler form. The simplest
carbohydrates are the three carbon dihydroxyacetone and trioses
glyceraldehyde. They are further classified into glucose, fructose, galactose, and
mannose.

Few common types of carbohydrates are milk, bread, popcorn, potatoes, maze, etc. 1.
Monosaccharides:
Monosaccharides are simple sugars. They cannot be hydrolyzed into a simpler form. The
simplest carbohydrates are the three carbon dihydroxyacetone and trioses glyceraldehyde.
They are further classified into glucose, fructose, galactose, and mannose.
Glucose:
Glucose can be seen generally in the fruit juices and formed in the body by hydrolysis of
cane sugar, starch, lactose, and maltose. Glucose is said to be the sugar of the body.
Glucose structure can be depicted in the form of a ring or chain. It is found in blood, fruits,
honey and under abnormal conditions, in urine.

Fructose:

Fructose can be seen naturally in honey, tomatoes, and apples. Hydrolysis of cane sugar in
the body can also give up fructose. C6H12O6 is the molecular formula for fructose. Generally,
fructose is the sweetest monosaccharide and is prepared by sucrose hydrolysis

Galactose:

An element of glycoproteins and glycolipids is the galactose. It is produced in the mammary

glands and hydrolyzed to make the lactose of milk.

Mannose:

On the hydrolysis of plant gums and mannosans, mannose is obtained. A constituent of the
prosthetic polysaccharide of albumins, mucoproteins, and globulins is a mannose. Hexoses
and pentoses exist in both ring and open chain forms.

2. Glycosaminoglycans (GAGs) or mucopolysaccharides are long linear

polysaccharides consisting of repeating disaccharide units (i.e. two-sugar units).
... Because GAGs are highly polar and attract water, they are used in the body as
a lubricant or shock absorber.
The acidic glycosaminoglycans (mucopolysaccharides) form an important
constituent of the connective tissue and have the general role in supporting and
binding together the cells to form tissues, the tissues to form organs and the further
organization of the organs into the systems of the body
3. Polysaccharides are complex biomacromolecules that are made up chains of
monosaccharides. The bonds that form these chains are glycosidic bonds.
Commonly found monomer units in polysaccharides are glucose, fructose,
mannose and galactose which are simple sugars.

 Homo-polysaccharides – are made up of one type of monosaccharide units. ex:

cellulose, starch, glycogen.
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 Hetero-polysaccharides – are made up of two or more types of monosaccharide units.

ex. hyaluronic acid and they provide extracellular support for organisms.
4. When sucrose is hydrolyzed it forms a 1:1 mixture of glucose and fructose. ... It is
called invert sugar because the angle of the specific rotation of the plain polarized
light changes from a positive to a negative value due to the presence of the
optical isomers of the mixture of glucose and fructose sugars.
5.

6. Starch is composed of two types of polymer chains known as amylose and

amylopectin. Amylose possesses a linear structure with α1–4 glycosidic
linkage while amylopectin possesses a branched structure with α1–4 as well as
α1–6 glycosidic linkages.
The functional properties of starch granules include swelling power, starch solubility,
gelatinization, retrogradation, syneresis, and rheological behaviour, which are
generally determined by the multiple characteristics of starch structure.
7. Osazone Formation: The reaction between three moles of phenylhydrazine and
one mole of aldose produces a crystalline product known as phenylosazone
(Scheme 1). ➢ Phenylosazones crystallize readily (unlike sugars) and are useful
derivatives for identifying sugars.
Principle. Phenyl hydrazine reacts with reducing sugar in an acidic environment at
high temperature to form phenylhydrazone. Phenyl hydrazine further reacts with the
sugar on heating and forms crystals of osazone specific to that carbohydrate
8. Inulin is a type of dietary fiber. Research has linked it to several health benefits,
such as improving digestive health, helping control diabetes, and aiding weight
loss. Inulin is a dietary fiber that may benefit gut health. Plants naturally contain
inulin, and some manufacturers add it to processed foods.
Dextran is a low molecular weight dextran used as an adjunctive treatment of shock
or impending shock due to hemorrhage, burns, surgery or other trauma, as well as
the prophylaxis of venous thrombosis and pulmonary embolism during high-risk
medical procedures
9. SUCROSE: Sucrose is extracted and refined by humans for food preparation. It is
commonly known as table sugar that is used as a sweetening agent for food and
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beverages. Organisms feed on sucrose for its monosaccharide constituents. By

digestion or hydrolysis, sucrose provides the organism glucose and fructose
Sucrose is made up of one molecule of glucose and one molecule of fructose joined
together. It is a disaccharide, a molecule composed of two monosaccharides:
glucose and fructose. Sucrose is produced naturally in plants, from which table sugar
is refined. It has the molecular formula C12H22O11.

MALTOSE: Maltose is a disaccharide consisting of two units of glucose. It has a

slightly sweet taste but digestion is its most important function. Since most
carbohydrates are in a non-absorbable shape, it is essential that these carbohydrates
are broken into smaller parts.
maltase, enzyme that catalyzes the hydrolysis of the disaccharide maltose to the
simple sugar glucose. The enzyme is found in plants, bacteria, and yeast; in humans
and other vertebrates it is thought to be synthesized by cells of the mucous
membrane lining the intestinal wall.

LACTOSE: Lactose is composed of glucose and galactose, two simpler sugars

used as energy directly by our body. Lactase, an enzyme, splits lactose into glucose
and galactose. Galactose is a component of several macromolecules (, which are
important constituents of nerve cells membrane.
Lactose is milk sugar. It's not as sweet as table sugar, but like table sugar,
lactose provides your cells with energy when you eat it. You can use lactose for a
number of other purposes, all of which it has in common with other carbohydrates
like table sugar and starch.
10. Sugar derivatives are modified monosaccharides. In sugar derivatives, the
monosaccharide molecules that have been modified with substituents other than
hydroxyl groups such as amino groups, acid groups, phosphate groups, acetate
groups etc. Natural sugar derivatives have important biological functions.
Most sugar derivatives occur naturally and have important biological functions. ... For
instance, amino sugar heparin occurs in intracellular granules of mast cells that line
arterial walls and, when released, inhibits blood clotting. Glycosylamine adenosine is
an important part of DNA and RNA structure
11. STARCH: Most starch is composed of two major polysaccharides: amylose and
amylopectin. Amylose is a primarily linear polysaccharide of α-1,4-linked d-
glucopyranose with a few branches of α-1,6 linkages.
The basic chemical formula of the starch molecule is (C6H10O5)n. Starch is a
polysaccharide comprising glucose monomers joined in α 1,4 linkages. The simplest
form of starch is the linear polymer amylose; amylopectin is the branched form.
GLYCOGEN: Glycogen is a branched polymer of glucose. Glucose residues are
linked linearly by α-1,4 glycosidic bonds, and approximately every ten residues a
chain of glucose residues branches off via α-1,6 glycosidic linkages. The α-glycosidic
bonds give rise to a helical polymer structure
12. Lipids are organic compounds that are fatty acids or derivatives of fatty acids,
which are insoluble in water but soluble in organic solvents. For eg., natural oil,
steroid, waxes. Lipids are molecules that contain hydrocarbons and make up the
building blocks of the structure and function of living cells. Examples of lipids
include fats, oils, waxes, certain vitamins, hormones and most of the cell
membrane that is not made up of protein.
Lipids include fats, oils, waxes, phospholipids, and steroids.
e.g., glycerophospholipids: fatty acids, glycerol, and headgroup
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13. Fatty acids are classified according to the presence and number of double bonds
in their carbon chain. Saturated fatty acids (SFA) contain no double bonds,
monounsaturated fatty acids (MUFA) contain one, and polyunsaturated fatty
acids (PUFA) contain more than one double bond.
Plasticity: Solid fats do not melt immediately
Flakiness: Fats help separate the layers of glut
Glazing: Fats give a glossy appearance to food,
Unsaturated fatty acids can also be classified as "cis" (bent form) or "trans" (straight
form), depending on whether hydrogen is bound on the same, or on the opposite side of
the molecule. Most naturally occurring unsaturated fatty acids are found in cis form
14. A phospholipid is a type of lipid molecule that is the main component of the cell
membrane. ... Each phospholipid is made up of two fatty acids, a phosphate
group, and a glycerol molecule. When many phospholipids line up, they form a
double layer that is characteristic of all cell membranes.
There are two types of phospholipids

 Glycerophospholipids: They are the major types of phospholipids, which

occur in the biological membrane. It consists of glycerol-based phospholipids.
 Sphingophospholipids: They are the important constituents of myelin and are
abundantly found in the brain and nervous tissues. It consists of sphingosine
as alcohol
15. The different levels of protein structure are known as primary, secondary, tertiary,
and quaternary structure. The primary structure is the sequence of amino acids
that make up a polypeptide chain. 20 different amino acids are found in proteins.
A protein's primary structure is defined as the amino acid sequence of its
polypeptide chain; secondary structure is the local spatial arrangement of a
polypeptide's backbone (main chain) atoms; tertiary structure refers to the three-
dimensional structure of an entire polypeptide chain; and quaternary structure is the
three-dimensional arrangement of the subunits in a multi subunit protein.
16. Classification of Amino Acids
 Glycine (H)
 Alanine (CH3)
 Valine (CH (CH3)2)
 Methionine (CH2CH2SCH3)
 Leucine (CH2CH(CH3)2)
 Isoleucine (-CH(CH3) CH2CH3)
 Proline (special structure)
 Phenylalanine.
Di-amino Acids: - Amino acids having amino group in the side chain.
Examples are: lysine, arginine and histidine. Aromatic amino acids:- Amino
acids containing aromatic side chains, examples: phenylalanine, tyrosine and
tryptophan. Imino acids: – Amino acids containing secondary amino acids like
proline
17. They are classified into three types; fibrous, globular and derived protein.
 Fibrous protein: They are elongated or fibre like protein
 Globular protein: They are spherical or globular in shape
 Derived protein: They are derivatives or degraded products of simple and
conjugated proteins.
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Based on the chemical nature, structure, shape and solubility, proteins are classified as:

 Simple proteins: They are composed of only amino acid residue.

 Conjugated proteins: They are combined with non-protein moiety.
 Derived proteins: They are derivatives or degraded products of simple and
conjugated proteins.

18. They are classified into three types; fibrous, globular and derived protein A
fibrous protein is one of the three main types of proteins. The others are globular
and membrane proteins). There are many types such as keratin, collagen,
elastin, and fibroin. Examples of fibrous proteins are α-keratin,the major
component of hair and nails, and collagen, the major protein component of
tendons, skin, bones, and teeth.
Globular: proteins are named for their approximately spherical shapes and are
the most abundant proteins in nature. The globular proteins exist in an enormous
variety of three-dimensional structures. Hydrophilic amino acid side chains lie on
the surface of the globular proteins exposed to the water. The example of
globular protein is haemoglobin which is considered as the member of the globin
protein family
derived proteins: are derivatives of proteins. These proteins are obtained from
simple or conjugated proteins as a result of partial hydrolysis by the action of
acids, enzymes or alkalies. These are called derivative proteins.
Examples include such foods as meat, eggs, milk and soybeans

19. The α helix, a common structural motif of proteins, consists of a right-handed

helix with a repeat length of 3.6 amino acid residues per helical turn. The α helix
is stabilized by hydrogen bonds between an amide hydrogen of one amino acid
and a carbonyl oxygen four amino acids away.
example, insulin (a globular protein) has a combination of hydrogen bonds and
disulfide bonds that cause it to be mostly clumped into a ball shape. ... Silk (a
fibrous protein), however, has a β-pleated sheet structure that is the result of
hydrogen bonding between different chains.
20. The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular
protein secondary structure. Beta sheets consist of beta strands (β-strands)
connected laterally by at least two or three backbone hydrogen bonds, forming a
generally twisted, pleated sheet.
Beta pleated sheet is an example of the secondary structure of a protein. The
beta sheet is composed of beta strands which are polypeptides linked by
hydrogen bonding. Beta strands have a 2 residues repeat and when the
polypeptide is fully extended, the distance between adjacent amino acids is 3.5 A
21. Albumin functions primarily as a carrier protein for steroids, fatty acids, and
thyroid hormones in the blood and plays a major role in stabilizing extracellular
fluid volume by contributing to oncotic pressure (known also as colloid osmotic
pressure) of plasma.
One of albumin's functions is to maintain colloid osmotic pressure, which keeps
fluid moving throughout the body. Albumin also helps metabolize and detoxify
substances (such as bilirubin, metals, ions, enzymes, amino acids, hormones,
free fatty acids, drugs, and phospholipids) and is a free-radical scavenger.
22. The isoelectric point (pI) is the pH at which a particular molecule carries no net
electrical charge. ... It is important to note that the calculation of the pI for a
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protein purely based on its amino acid sequence is often imprecise, since protein
folding, modification and also labelling can influence the pI.
The isoelectric point is significant in protein purification because it represents the
pH where solubility is typically minimal. Here, the protein isoelectric point signifies
where mobility in an electro-focusing system is zero—and, in turn, the point
where the protein will collect
23. Peptides are biologically and medically important molecules. ... Examples of
peptides include the hormone oxytocin, glutathione (stimulates tissue growth),
melittin (honey bee venom), the pancreatic hormone insulin, and glucagon (a
hyperglycaemic factor)
Peptides are biologically and medically important molecules. They naturally occur
within organisms, plus lab-synthesized compounds are active when introduced
into a body. Peptides act as structural components of cells and tissues,
hormones, toxins, antibiotics, and enzymes.
24. Nonstandard amino acids refer to those amino acids that have been chemically
modified after they have been incorporated into a protein (called a
“posttranslational modification”) and those amino acids that occur in living
organisms but are not found in proteins. Non-standard amino acids that are found
in proteins are formed by post-translational modification, which is modification
after translation during protein synthesis. These modifications are often essential
for the function or regulation of a protein
25. Blood proteins, also termed plasma proteins, are proteins present in blood
plasma. They serve many different functions, including transport of lipids,
hormones, vitamins and minerals in activity and functioning of the immune
system. ... All blood proteins are synthesized in liver except for the gamma
globulins.
Plasma proteins, such as albumin and globulin, that help maintain the colloidal
osmotic pressure at about 25 mmHg. Electrolytes like sodium, potassium,
bicarbonate, chloride, and calcium help maintain blood pH. Immunoglobulins help
fight infection and various other small amounts of enzymes, hormones, and
vitamins.
26. An enzyme is a substance that acts as a catalyst in living organisms, regulating
the rate at which chemical reactions proceed without itself being altered in the
process.
Nearly all enzymes end with the suffix of “-ase.” Generally, the names are of the
form “substrate or product – reaction catalyzed.” For example, lactate
dehydrogenase is for an enzyme that removes a hydrogen (plus 2e–, i.e., a
hydride) from lactate, yielding the carbonyl in pyruvate.
There were six classes of enzymes that were created so that enzymes could
easily be named. These classes are: Oxidoreductases, Transferases,
Hydrolases, Lyases, Isomerases, and Ligases.
27. Enzyme inhibition refers to a decrease in enzyme-related processes, enzyme
production, or enzyme activity. ... CYP450 inhibitors are different in their
selectivity toward enzymes and are classified by their mechanisms of action.
An enzyme inhibitor is a molecule that binds to an enzyme and decreases
its activity. By binding to enzymes' active sites, inhibitors reduce the compatibility
of substrate and enzyme and this leads to the inhibition of Enzyme-Substrate
complexes' formation, preventing the catalysis of reactions and decreasing (at
times to zero) the amount of product produced by a reaction.
28. There are three types of inhibitors; competitive and non-competitive inhibitor and
uncompetitive inhibitors. Competitive inhibitors bind to the active site of the
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enzyme and prevent substrate from binding. They can be, however, dissociated
with the addition of more substrates.
Competitive inhibitors compete with the substrate at the active site, and therefore
increase Km (the Michaelis-Menten constant). However, Vmax is unchanged
because, with enough substrate concentration, the reaction can still complete.
The graph plot of enzyme activity against substrate concentration would be
shifted to the right due to the increase of the Km, whilst the Lineweaver-Burke
plot would be steeper when compared with no inhibitor.
Non-Competitive Inhibitors Non-competitive inhibitors bind to another location on
the enzyme and as such decrease VMAX. However, KM is unchanged. This is
demonstrated by a lower maximum on a graph plotting enzyme activity against
substrate concentration and a higher y-intercept on a Lineweaver-Burke plot
when compared with no inhibitor.
29. Isozymes (also known as isoenzymes) are homologous enzymes that catalyze
the same reaction but differ in structure. ... The level of the different isozymes in a
certain organ is related to the level of oxygen supply. Isozymes appear in specific
regions of the body; differing in specifics organelles or tissues.
Isoenzymes are alternative forms of the same enzyme activity that exist in
different proportions in different tissues. Isoenzymes differ in amino acid
composition and sequence and multimeric quaternary structure; mostly, but not
always, they have similar (conserved) structures.
in recent years the determination of serum enzyme activities has played an
increasing role in clinical chemical diagnosis. ... Each serum enzyme can be
separated into isoenzymes which stem from different organs and make specific
organ diagnoses possible.
30. Koshland's induced fit theory
Induced fit theory was pro-posed by Koshland. Proteins are not rigid. The
substrate induces the enzyme to adjust its shape leading to the formation of
enzyme substrate complex
Fischer's Lock and key theory
Lock and key theory was proposed by Fisher. According to this theory, first a
physical contact is made between the enzyme and the substrate. As only a
specific key fits in a particular lock to open it, a specific substrate combines with
the active site of specific enzyme. This combination leads to the production of
enzyme - substrate complex.
31. Enzyme activity can be affected by a variety of factors, such as temperature, pH,
and concentration. Enzymes work best within specific temperature and pH
ranges, and sub-optimal conditions can cause an enzyme to lose its ability to bind
to a substrate.
Factor # 1. Concentration of Enzyme: As the concentration of the enzyme is
increased, the velocity of the reaction proportionately increases (Fig. 66.1). In
fact, this property of enzyme is made use in determining the activities of serum
enzymes for diagnosis of diseases.
Factor # 2. Concentration of Substrate: Increase in the substrate concentration
gradually increases the velocity of enzyme reaction within the limited range of
substrate levels. A rectangular hyperbola is obtained when velocity is plotted
against the substrate concentration. Three distinct phases of the reaction are
observed in the graph.
Factor # 3. Effect of Temperature: The optimum temperature for most of the
enzymes is between 40°C-45°C. In general, when the enzymes are exposed to a
temperature above 50°C, denaturation leading to derangement in the native
(tertiary) structure of the protein and active site are seen. Majority of the enzymes
become inactive at higher temperature.
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Factor # 4. Effect of pH: Increase in the hydrogen ion concentration (pH)

considerably influences the enzyme activity and a bell-shaped curve is normally
obtained Each enzyme has an optimum pH at which the velocity is maximum
Factor # 5. Effect of Product Concentration: The accumulation of reaction
products generally decreases the enzyme velocity. For certain’ enzymes, the
products combine with the active site of enzyme and form a loose complex and,
thus, inhibit the enzyme activity.
32. the 3-dimensional double helix structure of DNA, correctly elucidated by James
Watson and Francis Crick. ... DNA is a double-stranded helix, with the two
strands connected by hydrogen bonds. A bases are always paired with Ts, and
Cs are always paired with Gs, which is consistent with and accounts for
Chargaff's rule.
Three major forms of DNA are double stranded and connected by interactions
between complementary base pairs. These are terms A-form, B-form,and Z-form
DNA
DNA polymorphisms are the different DNA sequences among individuals, groups,
or populations. Polymorphism at the DNA level includes a wide range of
variations from single base pair change, many base pairs, and repeated
sequences. ... DNA polymorphisms are endless, and more discoveries continue
at a rapid rate
33. MRNA: Messenger RNA (mRNA) is a single-stranded RNA molecule that is
complementary to one of the DNA strands of a gene. The mRNA is an RNA
version of the gene that leaves the cell nucleus and moves to the cytoplasm
where proteins are made.
Messenger RNAs (mRNAs) are single-stranded molecules in cells that transfer
genetic information from the DNA in the nucleus to the cytoplasm, where proteins
are synthesized (in the ribosomes). mRNAs are a group of RNAs that can be
translated into proteins, while other RNAs cannot
The tRNA: molecule has a distinctive folded structure with three hairpin loops that
form the shape of a three-leafed clover. One of these hairpin loops contains a
sequence called the anticodon, which can recognize and decode an mRNA
codon. Each tRNA has its corresponding amino acid attached to its end.
Transfer ribonucleic acid (tRNA) is a type of RNA molecule that helps decode a
messenger RNA (mRNA) sequence into a protein. tRNAs function at specific
sites in the ribosome during translation, which is a process that synthesizes a
protein from an mRNA molecule.
rRNA: Ribosomal RNA (rRNA) associates with a set of proteins to form
ribosomes. These complex structures, which physically move along an mRNA
molecule, catalyse the assembly of amino acids into protein chains. They also
bind tRNAs and various accessory molecules necessary for protein synthesis.
Ribosomal RNA is the predominant form of RNA found in most cells; it makes up
about 80% of cellular RNA despite never being translated into proteins
itself. Ribosomes are composed of approximately 60% rRNA and 40% ribosomal
proteins by mass.
34. in molecular biology, DNA replication is the biological process of producing two
identical replicas of DNA from one original DNA molecule. DNA replication occurs
in all living organisms acting as the most essential part for biological inheritance.
The first category includes purine and pyrmidine nucleoside analogs that directly
inhibit DNA polymerase activity. The second category includes DNA damaging
agents including cisplatin and chlorambucil that modify the composition and
structure of the nucleic acid substrate to indirectly inhibit DNA synthesis.
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