BIOCHEMISTRY AND ITS ROLE IN DISEASE DIAGNOSIS

SESSION
GUIDED BY :-- 2008-09 SUBMITTED BY:-
Dr. A.K. Dwivedi Aditya Gulati
B.H.M.S. M.D. Ankush vani
H.O.D. Physiology Jagdeesh parmar
Rajesh sankhla
Sanju rathore.
INTRODUCTION
TO
BIOCHEMISTRY
BIOCHEMISTRY deals with
the chemical prosess taking
place in all living organisms
from smallest viruses to
bacteria to largest living
matter.
It is defined as , THE study of
chemical composition of
living matter and chemical
changes that occur in it
during life process.
HSTORY:
First intrdused by CARL
NEWBERG,a germen scientist in1903.
Concept was given by:Karl william
scheel
INCLUDES study of
Carbohydrates
Protiens,aminoacids,peptide
s
Lipids
Enzymes
INTRODUCTION TO
ENZYMES
Enzymes are biological catalysts
responsible for supporting almost all of the
chemical reactions that maintain animal
homeostasis. Because of their role in
maintaining life processes, the assay and
pharmacological regulation of enzymes
have become key elements in clinical
diagnosis and therapeutics.
 The macromolecular components of almost all
enzymes are composed of protein, except for a
class of RNA modifying catalysts known as
ribozymes. Ribozymes are molecules of
ribonucleic acid that catalyze reactions on the
phosphodiester bond of other RNAs.
 Enzymes are found in all tissues and fluids of
the body. Intracellular enzymes catalyze the
reactions of metabolic pathways.
 Plasma membrane enzymes regulate catalysis
within cells in response to extracellular
signals,
 and enzymes of the circulatory system are
responsible for regulating the clotting of blood
 Almost every significant life process is
dependent on enzyme activity.
 Enzyme Classifications
 Currently enzymes are grouped into six
functional classes by the International Union
of Biochemists (I.U.B.).
Number Classification Biochemical Properties

1 Oxidoreductases Act on many chemical groupings to add or

remove hydrogen atoms.

2 Transferases Transfer functional groups between donor

and acceptor molecules. Kinases are
specialized transferases that regulate
metabolism by transferring phosphate
from ATP to other molecules.
3 Hydrolases Add water across a bond, hydrolyzing it.

4 Lyases Add water, ammonia or carbon dioxide across

double bonds, or remove these elements to
produce double bonds.

5 Isomerases Carry out many kinds of isomerization: L to D

isomerizations, mutase reactions (shifts of
chemical groups) and others.
 Ligases Catalyze reactions in
6 which two chemical
groups are joined (or
ligated) with the use of
energy from ATP.
 Enzymes are also classified on the basis of
their composition. Enzymes composed wholly
of protein are known as simple enzymes in
contrast to complex enzymes, which are
composed of protein plus a relatively small
organic molecule. Complex enzymes are also
known as holoenzymes.
 In this terminology the protein component is
known as the apoenzyme, while the non-
protein component is known as the coenzyme
 Many prosthetic groups and coenzymes are
water-soluble derivatives of vitamins. It should
be noted that the main clinical symptoms of
dietary vitamin insufficiency generally arise
from the malfunction of enzymes, which lack
sufficient cofactors derived from vitamins to
maintain homeostasis.
 Enzymes that require a metal in their
composition are known as metalloenzymes
 Introduction - Enzyme Characteristics:
The basic mechanism by which enzymes catalyze chemical reactions
begins with the binding of the substrate (or substrates) to the active site on
the enzyme. The active site is the specific region of the enzyme which
combines with the substrate. The binding of the substrate to the enzyme
causes changes in the distribution of electrons in the chemical bonds of the
substrate and ultimately causes the reactions that lead to the formation of
products. The products are released from the enzyme surface to regenerate
the enzyme for another reaction cycle.
 The active site has a unique geometric shape that is
complementary to the geometric shape of a substrate molecule,
similar to the fit of puzzle pieces. This means that enzymes
specifically react with only one or a very few similar
compounds.
Lock and Key Theory:
The specific action of an enzyme with a single substrate can be
explained using a Lock and Key analogy first postulated in
1894 by Emil Fischer. In this analogy, the lock is the enzyme
and the key is the substrate. Only the correctly sized key
(substrate) fits into the key hole (active site) of the lock
(enzyme).
 Smaller keys, larger keys, or incorrectly positioned
teeth on keys (incorrectly shaped or sized substrate
molecules) do not fit into the lock (enzyme). Only the
correctly shaped key opens a particular lock. This is
illustrated in graphic on the left.
QUES: Using a diagram and in your own words,
describe the various lock and key theory of enzyme
action in relation to a correct and incorrect substrate.
 Induced Fit Theory:
Not all experimental evidence can be
adequately explained by using the so-called
rigid enzyme model assumed by the lock and
key theory. For this reason, a modification
called the induced-fit
theory has been proposed.
The induced-fit theory assumes that the substrate play
a role in determining the final shape of the enzyme an
that the enzyme is partially flexible. This explains why
certain compounds can bind to the enzyme but do not
react because the enzyme has been distorted too muc
Other molecules may be too small to induce the prope
alignment and therefore cannot react. Only the proper
substrate is capable of inducing the
Induced Fit Theory:
Not all experimental evidence can be adequately explained by using the so-
called rigid enzyme model assumed by the lock and key theory. For this reason,
a modification called the induced-fit theory has been proposed.
The induced-fit theory assumes that the substrate plays a role in determining
the final shape of the enzyme and that the enzyme is partially flexible. This
explains why certain compounds can bind to the enzyme but do not react
because the enzyme has been distorted too much. Other molecules may be too
small to induce the proper alignment and therefore cannot react. Only the
proper substrate is capable of inducing the proper alignment of the active site.
In the graphic on the left, the substrate is represented by the magenta
molecule, the enzyme protein is represented by the green and cyan colors. The
cyan colored protein is used to more sharply define the active site. The protein
chains are flexible and fit around the substrate.
 Enzymes in the
Diagnosis of Pathology
The measurement of the serum levels of numerous
enzymes has been shown to be of diagnostic
significance. This is because the presence of these
enzymes in the serum indicates that tissue or
cellular damage has occurred resulting in the
release of intracellular components into the blood.
Hence, when a physician indicates that he/she is
going to assay for liver enzymes, the purpose is to
ascertain the potential for liver cell damage.
Commonly assayed enzymes are the amino
transferases: alanine transaminase, ALT (sometimes
still referred to as serum glutamate-pyruvate
aminotransferase, SGPT) and aspartate
aminotransferase, AST (also referred to as serum
glutamate-oxaloacetate aminotransferase, SGOT);
lactate dehydrogenase, LDH; creatine kinase, CK (also
called creatine phosphokinase, CPK); gamma-glutamyl
transpeptidase, GGT. Other enzymes are assayed
under a variety of different clinical situations but they
will not be covered here.
The typical liver enzymes measured are AST and ALT. ALT
is particularly diagnostic of liver involvement as this
enzyme is found predominantly in hepatocytes. When
assaying for both ALT and AST the ratio of the level of
these two enzymes can also be diagnostic. Normally in
liver disease or damage that is not of viral origin the ratio
of ALT/AST is less than 1. However, with viral hepatitis the
ALT/AST ratio will be greater than 1. Measurement of AST
is useful not only for liver involvement but also for heart
disease or damage.
The level of AST elevation in the serum is directly proportional
to the number of cells involved as well as on the time
following injury that the AST assay was performed. Following
injury, levels of AST rise within 8 hours and peak 24-36 hours
later. Within 3-7 days the level of AST should return to pre-
injury levels, provided a continuous insult is not present or
further injury occurs. Although measurement of AST is not, in
and of itself, diagnostic for myocardial infarction, taken
together with LDH and CK measurements (see below) the
level of AST is useful for timing of the infarct.
 The measurement of LDH is especially diagnostic for myocardial
infarction because this enzyme exist in 5 closely related, but slightly
different forms (isozymes). The 5 types and their normal distribution
and levels in non-disease/injury are listed below.

LDH 1 - Found in heart and red-blood cells and is 17% - 27% of the
normal serum total.
LDH 2 - Found in heart and red-blood cells and is 27% - 37% of the
normal serum total.
LDH 3 - Found in a variety of organs and is 18% - 25% of the normal
serum total.
LDH 4 - Found in a variety of organs and is 3% - 8% of the normal
serum total.
LDH 5 - Found in liver and skeletal muscle and is 0% - 5% of the
normal serum total.
Following a myocardial infarct the serum levels of LDH rise
within 24-48 hours reaching a peak by 2-3 days and return to
normal in 5-10 days. Especially diagnostic is a comparison of
the LDH-1/LDH-2 ratio. Normally, this ration is less than 1. A
reversal of this ration is referred to as a "flipped LDH.".
Following an acute myocardial infart the flipped LDH ratio will
appear in 12-24 hours and is definitely present by 48 hours in
over 80% of patients. Also important is the fact that persons
suffering chest pain due to angina only will not likely have
altered LDH levels.
CPK is found primarily in heart and skeletal
muscle as well as the brain. Therefore,
measurement of serum CPK levels is a good
diagnostic for injury to these tissues. The levels of
CPK will rise within 6 hours of injury and peak by
around 18 hours. If the injury is not persistent the
level of CK returns to normal within 2-3 days.
Seminar Presentation
On
PROTEINS
BY
ANKUSH VANI
 INTRODUCTION
The proteins are complex molecules built mainly
from a-amino acid linked together in chains. The
linkage between the amino acids is called peptide
bond; molecules built up from many (up to 100)
amino acids are called polypeptides. Proteins
consist of several polypeptide chains, cross-
linkaged between specific amino acid units.
Chains containing 2-10 amino acids are called
peptides.
 Amino Acids
The principal amino acids obtained by breakdown of proteins are:

Neutral amino acids - they contain one NH2 (basic) group and one COOH (acidic)
group which mutually neutralize each other.

Types:

Amino acids with unsubstantiated C chains:

glycine, almandine, valine, leucine, isolucine.

(ii) Hydroxyl-substituted amino acids:

serine, threonine.

(iii) Sulphur containing amino acids:

cytosine, cystine (oxidative product of cytosine), methionine.

(iv) Aromatic amino acids, derived from almandine:

phenylalanine, tyrosine,thyroxine, triiodothyro-nine
2. Acidic amino acids - amino acids with acidic side chain:
aspartic acid, asparagine, glutamic acid, glutamine.

3. Basic amino acids - amino acids with basic side chain:

arginine, lysine, histidine.

4. Imino acids - contains imino group but no amino group:

proline, hydroxyproline.
 C. Digestion and absorption of proteins.
Digestion of proteins in the stomach
pepsin is the most important proteolytic enzyme of gastric
juiceOptimum pH for the activite of pepsin is 2 to 3 and it is
completely inactive at a pH above 5 . The hydrochloric acid in
the gastric juice provides the ideal pH for the activity of pepsin .

Pepsin acts on proteins and breaks them down into

proteoses , peptones and large polypestides . So , the proteins
reach the duodenum in these forms along with chyme.
 Proteins
Pepsin
(Gastric Juice)
Proteoses Peptones Large polypeptides

Trypsin
Chymotrypsin
(Endopeptidases in
Pancreatic juice)

Dipeptides Tripeptides Polypeptides

Carboxy peptidase Peptidases

(Exopeptidase in (Succus
pancreatic juice entericus)

Amino acids
DIGESTION OF PROTEINS IN THE SMALL INTESTINE

Most of the p[roteins are digested in the doudenum and jejunum by

the proteolytic enzymes of the pancreatic juice and succus entericus.
Pancreatic juice contains trypsin, chymotrypsin and carboxy peptidases.
Trypsin and chymotrypsin are called endopeptidases as these two enzymes
break the interior bonds of the protein molecules. Both the enzymes act on
proteoses and peptones split then into dipeptide and tripeptide molecules are
absorbed directly into the epithelial cells of the mucosa of the small intestine.
Carboxypeptidase from pancreatic juice breaks the terminal bonds of
the protein molecules. So, it is called exopeptidase. By the activity of
carboxypeptidase, the dipeptides, tripeptides and the polypeptides are
converted into amino acids.
The last digestion of the proteins is by proteolytic enzymes present in
the succus entericus. It contains dipeptidases, tripeptidases and
aminopolypeptidases. These enzymes act on large polypeptides and some of
the left over dipeptides and tripeptides and convert these proteins into the
final stage of single amino acids, which can be easily absorbed.
Pancreatic juice contains two more enzymes namely, collagenase and
elastease. Collagenase acts on collagen and elastase acts on elastic fibers.
 ABSORPTION OF PROTEINS

The proteins are absorbed in the form of amino acids from small intestine.
The levoamino acids are actively absorbed by means of sodium co-transport, whereas,
the dextroamino acids are absorbed by means of facilitated diffusion.

The absorption of amino acids is faster in duodenum and jejunum and

slower in ileum.
D. Amino Acid Pool:-
Most of the tissue proteins (structural as well as functional
protein) are continuously undergoing disintegration to
release amino acids. The amino acids derived from food
(exogenous protein) and those derived from the tissues
break down (endogenous protein) enter the circulation
forming general ammo acid pool. It represents an
availability of amino acid building units. From this
common amino acid pool, amino acids are taken up by the
cells, if a cell takes up as much amino acid as it loses, it is in
a state of dynamic equilibrium; if the loss is greater, the cell
degenerates; if the gain is greater, the cell grows. The
proteins of the body are in a state of dynamic equilibrium
i.e. a balance between simultaneous breakdown and
synthesis. The endogenous protein turnover rate is about
80-100 gm/day being greatest in intestinal mucosa, followed
by kidney, liver, brain and muscle in that order.
E. Essential Amino acids

These are the amino acids needed for replacement and

growth, but which cannot be synthesized by the body in
amounts sufficient to fulfil its normal requirements. The
rest of the amino acids are the non-essential amino acids
and can be synthesized in the body. It has been found that
the following amino acids are indispensable for human
adults under normal conditions: valine, leucine, isoleucine,
threonine, methionine, phenylalanine, tryptophan, lysine,
histidine and arginine .
F. Specific Metabolic Roles of Amino Acids

1. Amino acids are the building units of all the tissue proteins including
the enzymes and many of the hormones.
2. Glycine is a fundamental building unit, and an inhibitory
transmitter in the spinal cord.
3. Arginine is responsible for urea formation and helps in creatine
synthesis.
4. Histidine is the precursor of histamine.
5. Phenylalanine can be irreversibly converted to tyrosine which is the
precursor for thyroxine, epinephrine, nor-epinephrine and melanin
pigment.
6. Tryptophan is essential for the formation of 5 HT (serotonin).
7. Methionine, cysteine and cystine are the only important source of
sulphur and are used for the forjnation of organic sulphates or
taurine.
G. Urinary Sulphates

The sulphur compounds of urine are derived mainly from the sulphur
containing amino acids (methionine, cysteine and cystine) of the dietary and
tissue proteins. The sulphur is excerted in urine in the following forms:
1. Inorganic sulphate :
Sulphur containing amino acids of the amino acid pool that are not used in
protein synthesis are completely oxidised and the sulphur as sulphate ions
(SO42~) are excreted in urine, with an equivalent amount of cations (Na+,
K+, NH4T). The normal range of urinary output is 0.3-3 gm of sulphate
ions /day.
2. Ethereal sulphate :
The urine contains small amounts of organic sulphate esters, R-O-
SO3H (ethereal sulphates), where R is the aromatic radicals. These
are the forms in which many phenols (oestrogen, steroids, indoles
and drugs like aspirin) are detoxicated and excreted in urine. The
conjugation of the phenol with sulphate from amino acids takes
place in the liver
3. Neutral sulphur e.g. cystine, mercaptans are found in the urine in
traces.
 METABOLISM OF AMINO ACIDS

[A] Metabolism of amino acids involve the following reactions:

1. Oxidative deamination : Amino acids which are not used as such undergo 'oxidative
deamination'/ primarily in the liver. The overall reaction is the transformation of an
amino acid R.CH(NH2).COOH, to the corresponding keto acid, R.CO.COOH. This
involves an oxidation (or dehydrogenation) to give a-imino acid, followed by
hydrolysis liberating 'ammonia'.
CH3.CH(NH2) COOH + NAD
Alanine coenzyme (H carrier)
amino acid oxidase
CH3.C(:NH)COOH + NAD.2H
-imino acid reduced coenzyme

CH,C (:NH) COOH + H,O

CH2.CO.COOH+NH3
pyruvic acid
The ammonia thus formed is then used up in the synthesis of other
amino acids or excreted as urea
2. Transamination

It is the process in which deamination of an amino acid to

corresponding ketoacid is coupled with the simultaneous amination
of another ketoacid to an amino acid e.g.

transaminase

Alanine + ot-keto-glutaric acid pyruvic acid + elutamic acid

(present in the circulation)

 Diet Body Inert protein
protein hair etc.

transamination
Urin Common
Amino acid pool Amination
excretion mettabolic
Deamination pool

NH4+
Creatine Purines Hormones Urea
Pyrimidines neurotransmitters

Amino acid metabolism

2. Transamination is 'reversible'. Thus plays an important role in
both the breakdown of amino-acids and their synthesis from non-
protein sources; for example, from ketoacids of the citric acid cycle.
3. Amination of non-nitrogenous residues
Amino-acids from the amino acid pool are continually being
broken down by deamination, and the processs of direct amination or
transamination are used to resynthesize some of these amino-acids.
Products of deamination formed at one site can be reaminated
elsewhere and so re-enter the 'amino acid pool'.
4. Ammonia
Ammonia formed by the kidney tubule cells, mainly from glutamine,
diffuses into the lumen of the tubules and act as a hydrogen ion
acceptor.
[B] Urea Formation
1. The excess of ammonia which is formed by deamination and not
used for reamination is converted into urea. Ammonia is very toxic to
cells whereas 'urea' is harmless even in very high concentrations. The
liver is the only site of urea formation, and that urea once formed is
not destroyed in the body.
2. Urea formation in the liver consists of the union of 2 moles of NH3
and one mole of CO2 with the elimination of H2O. This takes place
directly through the Krebs urea cycle in which 'non-protein' amino
acid ornithine acts as a catalyst to form citrulline (Fig. 8.4.2). This
reacts with a second mole of NH, to give arginine; the amidine group
of arginine is split off as urea by hydrolytic enzyme 'arginase', and
ornithine is regenerated to continue the cycle.
[C] Fate of non-nitrogenous residues from amino acids

The non-nitrogenous residues remaining .after

deamination enter the 'common metabolic pool' and are
either completely catabolised to CO., or are built up into
other body constituents.
In general, the essential amino acids are 'glucogenic' i.e.
they give rise to compounds that can readily be converted
to glucose; all the non-essential amino acids are 'ketogenic'
i.e. they give rise to ketone bodies.
Applied Aspect

In certain condition oxidative mechanisms of amino acid are

dearranged by the blockage at different point . This results in the
urinari excretion of intermediate metabalies For example:-
1. Phenylketonuria : It is a form of idiocy in which there is an inability
to convert phenylalamine to tyrosine therefore phenylalamine
accumulates, and phenyl-pyruvic acid (the deamination product of
phenylalanine) appears in the urine.

2. Alcaptonuria : Here, a normal metabolite from tyrosine appears in

the urine; such urine darkens considerably when alkaline is exposed to
air and may turn almost black.
[D] Significance of nitrogen containing constituents in urine

Mixed proteins contain an average of 16% of nitrogen, almost all of

which is excreted in the urine. The chief nitrogen containing waste
products in urine are: urea, creatinine, creatine, ammonium ions and
uric acid. A small amount of amino acids are also lost from the body
through the urine.

1. Urea - Urea is formed in the liver from ammonia derived from

amino-acids
(a) On a normal protein intake (the 'amino acid pool' is contributed by
the : ingested food), the urinary urea is mainly of food origin i.e.
exogenous proteins. Within limits, the urea output varies directly with
the recent protein intake. On a normal mixed diet, an adult's excretion
of urea is 15-50 gm/day (= 7-23 gm of urea nitrogen).
 (ii) On a protein-free diet but adequate in energy content, the
amino acids are contributed to the 'pool' by breakdown of tissue
proteins only i.e. endogenous proteins. Amino acids from this
endogenous proteins cannot be rebuilt into the proteins from which
they come, because one or more of the required essential amino acid
needed for the protein synthesis has been utilized elsewhere; moreover,
these amino acids cannot be stored and are irreversibly broken down
producing first ammonia and then urea which appears in the urine.
Thus, the urinary urea on a 'protein-free diet' is wholly 'endogenous'
and is approximately 4 gm of urea/day.
(iii) In complete starvation tissue protein (specially muscle protein) is
broken down into amino acids on a much larger scale than in (ii)
above. Most of this is deaminated and the residues utilized for energy
purposes and to maintain the blood sugar level. Therefore, urea
excretion is on a much larger scale because tissue protein is not being
used as "fuel".
2. Creatine and creatinine

(i) Creatine occurs in greatest concentration in skeletal muscle, with

lesser amounts in heart muscle, brain and uterus. In resting muscle,
creatine exists largely as creatine phosphate (phosphocreatine), a
high energy compound. This is formed by the reaction of creatine
with ATP (reversible reaction). The energy of carbohydrate
catabolism in muscle is initially made available as ATP which reacts
with creatine to form ADP and large amounts of creatine phosphate.
During exercise, the reaction is reversible, maintaining the supply of
ATP (an immediate source of energy for muscle contraction).
(ii) Creatine is synthesized in the liver from arginine, glycine and
methio-nine. Creatine gets phosphorylated by ATP to give creatine
phosphate, some of which lost to the body by a slow, spontaneous
transformation to 'creatinine' is excreted in urine.
(iii) Creatinuria i.e. excretion of creatine in urine. Creatine is not a normal
constituent of the urine but may. appear in the following conditions:
(a) In children, creatinuria may be associated with the low storage power of
the muscles for creatine at an early age.
(b) Pregnancy - There is a continuous creatinuria during pregnancy,
which rises to a maximum of 1.5 gm/day after delivery; when it is derived from
the involuting uterus.
(c) Myopathies - Creatinuria occurs because of the low storage power of the
muscles.
(d) In any condition in which unusual breakdown of the tissues (specially
muscles) occurs, e.g. in starvation (muscles substance is broken down for enerev
purposes), diabetes mellitus, goitre and fever (from the increased metabolic rate).

(iv) Excretion of creatinine - Creatinine is formed in the body exclusively from

creatine via creatine phosphate; therefore, the urinary output of creatinine
increases during exercise.
3. Ammonium ions (NH/)

4. Amino acids - traces of many amino acids and small peptides are
found in normal urine; mainly they come from the breakdown of
tissue protein
(endogenous excretion).

5. Uric acid - This is the only end product from the metabolism of purines
and nucleic acids which normally appear in the urine
 NUCLEIC ACID
[A] General
1. Purines
(i) The major purines found in nucleo-tides and nucleic acids are
adenine and guanine. 'Uric acid' is the final oxidation product of all
purines; intermediate oxidation products are hypoxanthine and
xanthine.
(ii) The diet contributes small amounts of 'free' purines to the body
from meat ^extract, tea, coffee and cocoa.

2.Pyrimidines
The major pyrimidines found in nucleotides and nucleic acid are
cytosine, uracil and thymine.
 Applied Aspect: GOUT
[A] Gout is characterised by:-

1 Excess of uric acid in the blood.

2. In normal persons 'metabolic pool' of uric acid is 0.7-1.3 gin which

increases to 2-4 gm.

3. Deposition of sodium monourate in articular and non-articular

structures, producing tophi.

4. Recurring attacks of acute arthritis. These are due to deposition of

microcrystals of monosodium urate in and around the structures of the
affected joints. The joint most commonly affected in early stages is
metatarsophalangeal joint of the great toe.
[B] Types: Primary and Secondary Gout

(i) Primary gout: Here, increased forma tion of uric acid occurs from
simple carbon and nitrogen compound without intermediary
incorporation into nucleic acids.

(ii) Secondary gout: There is an increased breakdown of nucleic acids

leading to an excess of the end-product, uric acid; it occurs in
polycythaemia, chronic leukaemias and pernicious anaemia.

[C] Treatment

a) Acute gout - The most effective drugs are colchicine,

phenylbutazone and indomethacin. They increase the renal excretion
of uric acid.
Chronic gout

a) Prolonged administration of drugs which increases the excretion of

uric acid in the urine
by decreasing tubular reabsorption of uric acid e.g. 'probenecid' and
'salicylates

b) 'Allopurinol' inhibits the enzyme xanthine oxidase and thus reduces

uric acid synthesis.
 Vitamin
A vitamin is an organic compound
required as a nutrient in tiny amounts by
an organism.
allowing supplementation of the dietary
intake.
 History

The discovery of vitamins and their structureYear of

discovery Vitamin Source1909Vitamin A (Retinol)Cod
liver oil1912Vitamin B1 (Thiamin)Rice bran1912Vitamin C (
Ascorbic acid)Lemons1918Vitamin D (Calciferol)Cod liver oil
1920Vitamin B2 (Riboflavin)Eggs1922Vitamin E (Tocopherol
)Wheat germ oil, Cosmetic and Liver1926Vitamin B12
(Cyanocobalamin)Liver1929Vitamin K (Phylloquinone)
Luzerne1931Vitamin B5 (Pantothenic acid)Liver1931Vitamin
B7 (Biotin)Liver1934Vitamin B6 (Pyridoxine)Rice bran
1936Vitamin B3 (Niacin)Liver1941Vitamin B9 (Folic acid)
Liver
 In humans there are 13 vitamins: 4 fat-soluble
(A, D, E and K) and 9 water-soluble (8 B
vitamins and vitamin C).
 Thiamin
PropertiesMolecular formula
C12H17N4OS+Molar mass265.356
Melting point248-260 C (hydrochloride salt)
 Thiamin or thiamine, also known as vitamin B1 and
aneurine hydrochloride, is the name of a family of
molecules sharing a common structural feature
responsible for its activity as a vitamin. It is one of
the B vitamins. Its most common form is a colorless
chemical compound with a chemical formula C12H17
N4OS. This form of thiamine is soluble in water,
methanol, and glycerol and practically insoluble in
acetone, ether, chloroform, and benzene. Another
form of thiamine known as TTFD has different
solubility properties and belongs to a family of
molecules often referred to as fat-soluble thiamines
 History
Thiamin was first discovered in 1910 by
Umetaro Suzuki in Japan when researching how rice
bran cured patients of beriberi. He named it aberic
acid (later oryzanin). He did not determine its
chemical composition, nor that it was an amine. It
was first crystallized by Jansen and Donath in 1926
(they named it aneurin, for antineuritic vitamin). Its
chemical composition and synthesis was finally
reported by Robert R. Williams in 1935.
 Sources
Yeast
Oatmeal
Brown rice
Whole grain flour (rye or wheat)
Asparagus
Kale
Cauliflower
Potatoes
Oranges
 Genetic diseases
Genetic diseases of thiamin transport are rare but
serious. Thiamin Responsive Megaloblastic Anemia
with diabetes mellitus and sensorineural deafness is
an autosomal recessive disorder caused by mutations
in the gene a high affinity thiamine transporter.
TRMA patients do not show signs of systemic
thiamin deficiency, suggesting redundancy in the
thiamin transport system. This has led to the
discovery of a second high affinity thiamin
transporter, SLC19A3.
 High doses
The RDA in most countries is set at about 1.4
mg. However, tests on volunteers at daily
doses of about 50 mg have claimed an increase
in mental acuity.
Riboflavin (
Vitamin B2)
 PropertiesMolecular formula
C17H20N4O6Molar mass376.36 g/mol
Melting point290 C (dec.)
 Riboflavin (E101), also known as vitamin
B2, is an easily absorbed micronutrient with a
key role in maintaining health in humans and
animals. It is the central component of the
cofactors FAD and FMN, and is therefore
required by all flavoproteins. As such, vitamin
B2 is required for a wide variety of cellular
processes.
 Toxicity
Riboflavin is not toxic when taken orally, as its
low solubility keeps it from being absorbed in
dangerous amounts from Although toxic doses
can be administered by injection, any excess at
nutritionally relevant doses is excreted in the
urine imparting a bright yellow color when in
large quantities.
 Nutrition
Riboflavin deficiency
Riboflavin is continuously excreted in the
urine of healthy individuals, making
deficiency relatively common when dietary
intake is insufficient. However, riboflavin
deficiency is always accompanied by
deficiency of other vitamins.
 Clinical Uses
Riboflavin has been used in several clinical
and therapeutic situations. For over 30 years,
riboflavin supplements have been used as part
of the phototherapy treatment of neonatal
jaundice. The light used to irradiate the infants
breaks down not only the toxin causing the
jaundice, but the naturally occurring riboflavin
within the infant's blood as well.
 Deficiencies Deficiencies of
vitamins are classified as either primary or
secondary. A primary deficiency occurs when
an organism does not get enough of the
vitamin in its food. A secondary deficiency
may be due to an underlying disorder that
prevents or limits the absorption or use of the
vitamin, due to a lifestyle factor, such as
 Side effects and overdose
In large doses, some vitamins have
documented side effects that tend to be more
severe with a larger dosage. The likelihood of
consuming too much of any vitamin from food
is remote, but overdosing from vitamin
supplementation does occur. At high enough
dosages some vitamins cause side effects such
as nausea, diarrhea, and vomiting.
 Niacin
Niacin, also known as vitamin B3, is a water-
soluble vitamin which prevents the
deficiency disease pellagra. It is an
organic compound with the molecular formula
C6H5NO2. It is a derivative of pyridine, with a
carboxyl group (COOH) at the 3-position. Other
forms of vitamin B3 include the corresponding
amide, nicotinamide ("niacinamide"), where the
carboxyl group has been replaced by an amide
group (CONH2), as well as more complex amides
and a variety of esters.
 History
Niacin was first described by Hugo Weidel in 1873 in
his studies of nicotine. The original preparation
remains useful: the oxidation of nicotine using nitric
acid Niacin was extracted from livers by
Conrad Elvehjem who later identified the active
ingredient, then referred to as the "pellagra-
preventing factor" and the "anti-blacktongue factor."
When the biological significance of nicotinic acid
was realized, it was thought appropriate to choose a
name to dissociate it from nicotine, in order to avoid
the perception that vitamins or niacin-rich food
contains nicotine.
 Toxicity
People taking pharmacological doses of niacin (1.5 -
6 g per day) often experience a syndrome of side-
effects that can include one or more of the following:
dermatological complaints
facial flushing and itching
dry skin
skin rashes including acanthosis nigricans
gastrointestinal complaints
dyspepsia (indigestion)
 liver toxicity
fulminates hepatic failure
hyperglycemia
cardiac arrhythmias
birth defects
orthostasis
 Pantothenic acid

 Pantothenic acid, also called vitamin B5 (a

B vitamin), is a water-soluble vitamin required
to sustain life (essential nutrient). Pantothenic
acid is needed to form coenzyme-A (CoA),
and is critical in the metabolism and synthesis
of carbohydrates, proteins, and fats.
 Sources
Daily requirement
Pantothenate in the form of pantethine is considered
to be the more active form of the vitamin in the body,
but is unstable at high temperatures or when stored
for long periods, so calcium pantothenate is the more
usual form of vitamin B5 when it is sold as a
dietary supplement. Ten mg of calcium pantothenate
is equivalent to 9.2 mg of pantothenic acid.
 Absorption
Within most foods, pantothenic acid is in the
form of CoA or acyl-carrier protein (ACP). In
order for the intestinal cells to absorb this
vitamin it must be converted into free
pantothenic acid. Within the lumen of the
intestine, CoA and ACP are degraded from the
food into 4'-phosphopantetheine. .
 Deficiency
Pantothenic acid deficiency is exceptionally
rare and has not been thoroughly studied. In
the few cases where deficiency has been seen
(victims of starvation and limited volunteer
trials), nearly all symptoms can be reversed
with the return of pantothenic acid.
 Toxicity
Toxicity of pantothenic acid is unlikely. Large doses
of the vitamin, when ingested, have no reported side
effects and massive doses (e.g. 10 g/day) may only
yield mild intestinal distress and diarrhea at worst.
There are also no adverse reactions known following
parenteral or topical application of the vitamin.
 Pyridoxine
PropertiesMolecular formulaC8H11NO3
Molar mass169.18 g/molMelting point159-162
C
 Pyridoxine is one of the compounds that can
be called vitamin B6, along with Pyridoxal and
Pyridoxamine. It differs from pyridoxamine by
the substituent at the '4' position. It is often
used as 'pyridoxine hydrochloride'
 Function in the body
Pyridoxine assists in the balancing of sodium and
potassium as well as promoting red blood cell
production. It is linked to cardiovascular health by
decreasing the formation of homocysteine. It has been
suggested that Pyridoxine might help children with
learning difficulties, and may also prevent dandruff,
eczema, and psoriasis. In addition, pyridoxine can
help balance hormonal changes in women and aid in
immune system.
 Medicinal uses
It is given to patients taking isoniazid to
combat the toxic side effects of the drug.
Pyridoxine is given 10-50 mg/day to patients
on INH (Isoniazid) to prevent
peripheral neuropathy and CNS effects that are
associated with the use of isoniazid.
 Biotin
Biotin
Properties Molecular formulaC10H16N2O3S
Molar mass244.31 g/molSolubility in waterSoluble

Biotin, also known as vitamin H or B7, has the

chemical formula C10H16N2O3S (Biotin; Coenzyme
R, Biopeiderm), is a water-soluble B-complex vitamin
which is composed of an ureido
(tetrahydroimidizalone) ring fused with a
tetrahydrothiophene ring. A valeric acid substituent is
attached to one of the carbon atoms of the
tetrahydrothiophene ring.
 Sources
Dietary
Recommended Adequate Intake* for
BiotinAgeBiotin (mcg/day)Infants06
months5712 months6Children13 years848
years12Males and Females913 years2014-18
years251970 years3070+
years30Pregnant<18-5030Lactating<18-
5035Uses
Hair Problems
Cradle cap (seborrheic dermatitis)
 Deficiency
Biotin deficiency is relatively rare and mild, and can be
addressed with supplementation. Such deficiency can be
caused by the excessive consumption of raw egg whites,
which contain high levels of the protein avidin, which
binds biotin strongly. Avidin is deactivated by cooking,
while the biotin remains intact.
Toxicity Animal
studies have indicated few, if any, effects due to
toxic doses of biotin. This may provide evidence
that both animals and humans may tolerate doses
of at least an order of magnitude greater than
each of their nutritional requirements.
 Vitamin B12
"B12" redirects here. For other uses, see
B12 (disambiguation).
Vitamin B12Systematic (IUPAC) name-(5,6-
dimethylbenzimidazolyl)cobamidcyanideTherapeutic
considerationsPregnancy cat.?Legal statusPOM(UK)
Routesoral, ivVitamin B-12 is a vitamin, one of eight
B vitamins which is important for the normal functioning of
the brain and nervous system, and for the formation of
blood. It is normally involved in the metabolism of every
cell of the body, especially affecting DNA synthesis and
regulation, but also fatty acid synthesis and energy
production.
 Systematic (IUPAC) name-(5,6-
dimethylbenzimidazolyl)cobamidcyanide Ther
apeutic considerationsPregnancy cat.?Legal
statusPOM(UK)Routesoral, iv
 Terminology
name vitamin B-12, known as vitamin B12
(commonly B12 or B-12 for short) generally refers to
all forms of the vitamin. Some medical practitioners
have suggested that its use be split into two different
categories, however.
In a broad sense B-12 still refers to a group of cobalt-
containing vitamer compounds known as cobalamins:
these include cyanocobalamin (an artifact formed as a
result of the use of cyanide in the purification
procedures), hydroxocobalamin (another medicinal
form), and finally, the two naturally occurring
cofactor forms of B-12: 5-deoxyadenosylcobalamin (
adenosylcobalaminAdoB-12), the cofactor of
Methylmalonyl Coenzyme A mutase (MUT), and
methylcobalamin (MeB-12), the cofactor of
5-methyltetrahydrofolate-homocysteine
methyltransferase (MTR).
 Structure
Vitamin B-12 is a collection of cobalt and corrin
ring molecules which are defined by their
particular vitamin function in the body. All of the
substrate cobalt-corrin molecules from which B-
12 is made must be synthesized by bacteria.
However, after this synthesis is complete, the
body has a limited power to convert any form of
B-12 to another, by means of enzymatically
removing certain prosthetic chemical groups from
the cobalt atom.
 Functions

Vitamin B-12 is normally involved in the metabolism of every

cell of the body, especially affecting the DNA synthesis and
regulation but also fatty acid synthesis and energy production.
However, many (though not all) of the effects of functions of
B-12 can be replaced by sufficient quantities of folic acid
(another B vitamin), since B-12 is used to regenerate folate in
the body. Most "B-12 deficient symptoms" are actually folate
deficient symptoms, since they include all the effects of
pernicious anemia and megaloblastosis, which are due to poor
synthesis of DNA when the body does not have a proper
supply of folic acid for the production of thymine. When
sufficient folic acid is available, all known B-12 related
deficiency syndromes normalize, save those narrowly
connected with the B-12 dependent enzymes Methylmalonyl
Coenzyme A mutase (MUT), and
5-methyltetrahydrofolate-homocysteine methyltransferase (
MTR), also known as methionine synthase;acid, MMA) and
homocysteine.
 Human absorption and distribution
The human physiology of vitamin B-12 is
complex, and therefore is prone to mishaps
leading to vitamin B-12 deficiency. The
vitamin as it occurs in foods enters the
digestive tract bound to proteins, known as
salivary R-binders. Stomach proteolysis of
these proteins requires an acid pH, and also
requires proper pancreatic release of
proteolytic enzymes referred to as pepsin.

 Clinical symptoms
: The main syndrome of vitamin B-12 deficiency is Biermer's
disease (pernicious anemia ). It is characterized by a triad of
symptoms:
Anemia with bone marrow promegaloblastosis ( Megaloblastic
anemia)
Gastrointestinal symptoms
Neurological symptoms
Each of those symptoms can occur either alone or along with others.
The neurological complex, defined as myelosis funicularis , consists
of the following symptoms:
Impaired perception of deep touch, pressure and vibration,
abolishment of sense of touch, very annoying and persistent
paresthesias .
 Sources
Foods
Vitamin B-12 is naturally found in meat (especially liver and
shellfish), milk and eggs. Animals, in turn, must obtain it
directly or indirectly from bacteria, and these bacteria may
inhabit a section of the gut which is posterior to the section
where B-12 is absorbed. Thus, herbivorous animals must
either obtain B-12 from bacteria in their rumens, or (if
fermenting plant material in the hindgut) by reingestion of
cecotrope fces. Eggs are often mentioned as a good B-12
source, but they also contain a factor that blocks
absorption.Certain insects such as termites contain B-12
produced by their gut bacteria, in a manner analogous to
ruminant animals.An NIH Fact Sheet lists a variety of food
sources of vitamin B-12.
 Other medical uses
Hydroxycobalamin, or hydoxocobalamin, also known
as Vitamin B-12a, is used in Europe both for vitamin
B-12 deficiency and as a treatment for cyanide
poisoning, sometimes with a large amount (5-10 g)
given intravenously, and sometimes in combination
with sodium thiosulfate.[45] The mechanism of
action is straightforward: the hydroxycobalamin
hydroxide ligand is displaced by the toxic cyanide
ion, and the resulting harmless B-12 complex is
excreted in urine.
 Folic acid
Properties

Molecular formulaC19H19N7O6Molar mass

441.403 g/molAppearanceyellow-orange
crystalline powderMelting point250 C (523 K),
decomp.Solubility in water0.0016 mg/ml (25
C)Acidity (pKa)1st: 2.3, 2nd: 8.3
 Folic acid and Folate are forms of the water-soluble
Vitamin B9. These occur naturally in food and can
also be taken as supplements. Folate gets its name
from the Latin word folium ("leaf").
History
A key observation by researcher Lucy Wills in 1931
led to the identification of folate as the nutrient
needed to prevent anemia during pregnancy. Dr. Wills
demonstrated that anemia could be reversed with
brewer's yeast. Folate was identified as the corrective
substance in brewer's yeast in the late 1930s and was
extracted from spinach leaves in 1941.
 Human reproduction
There are several important nutrients that serve as building
blocks of a healthy pregnancy. Two of the more well-known
nutrients for women during child bearing years are folic acid
and calcium (with Vitamin D). One nutrient that women are
not as familiar with is DHA ( docosahexaenoic acid) omega-3.
DHA is important for optimal infant brain, eye and nervous
system development, and has been shown to support a healthy
pregnancy. Folic acid is very important for all women who
may become pregnant. Adequate folate intake during the
periconceptional period, the time just before and just after a
woman becomes pregnant, helps protect against a number of
congenital malformations including neural tube defects.
 Some current issues and controversies
about folate
Dietary fortification of folic acid
Heart disease
Stroke
Cancer
Memory and mental agility
Fertility
 Ascorbic acid
(R)-3,4-dihydroxy-5-((S)- 1,2-dihydroxyethyl)furan-
2(5H)-one
 Properties Molecular formulaC6H8O6Molar mass176.1241
g/molAppearanceWhite or light yellow solidDensity1.65
g/cmMelting point190-192 C, 463-465 K, 374-378 F
(decomposes)Solubility in water33g/100mlSolubility in
ethanol2g/100mlSolubility in glycerol1g/100mlSolubility in
propylene glycol5g/100mlSolubility in
diethyl ether, chloroform, benzene, petroleum ether, oils, fats, f
at
solventsinsolubleAcidity (pKa)4.17 (first), 11.6
(second)Hazards MSDSScienceLab.comLD5011.9 g/kg (oral,
rat)[
 Uses

Ascorbic acid is easily oxidized and so is used

as a reductant in photographic developer
solutions (among others) and as a preservative.
Exposure to oxygen, metals, light, and heat
destroys ascorbic acid, so it must be stored in a
dark, cold, and non-metallic container.
The relevant European food additive
E numbers are:
Movement of electron pairs in deprotonation
 PropertiesMolecular formulaC20H30O
Molar mass286.456 g/mol
 E300 ascorbic acid,
E301 sodium ascorbate,
E302 calcium ascorbate,
E303 potassium ascorbate,
E304 fatty acid esters of ascorbic acid (i)
ascorbyl palmitate (ii) ascorbyl stearate.
It can be added to water that has been treated
with iodine to make it potable, neutralizing
the unpleasant iodine taste, and increasing the
health benefits of drinking water, although
increasing the chance of tooth decay.
Retinol
 Retinol (Afaxin), the animal form of
vitamin A, is a fat-soluble vitamin important in
vision and bone growth. It belongs to the
family of chemical compounds known as
retinoids. Retinol is ingested in a precursor
form; animal sources (liver and eggs) contain
retinyl esters, whereas plants (carrots, spinach)
contain pro-vitamin A carotenoids.
 Discovery
In 1913, Elmer McCollum, a biochemist at the
University of Wisconsin-Madison, and colleague
Marguerite Davis identified a fat-soluble nutrient in
butterfat and cod liver oil. Their work confirmed that
of Thomas Osborne and Lafayette Mendel, at Yale,
which suggested a fat-soluble nutrient in butterfat,
also in 1913.
Vitamin A was first synthesized in 1947 by two Dutch
chemists, David Adriaan van Dorp and Jozef
Ferdinand Arens.
 Clinical use
Main article: Tretinoin
All retinoid forms of vitamin A are used in cosmetic
and medical applications applied to the skin. Retinoic
acid, termed Tretinoin in clinical usage, is used in the
treatment of acne and keratosis pilaris in a topical
cream. An isomer of tretinoin, isotretinoin is also
used orally (under the trade names Accutane and
Roaccutane), generally for severe or
recalcitrant acne.
 Nutrition
Vitamin A deficiency is common in developing
countries but rarely seen in developed countries.
Approximately 250,000 to 500,000 malnourished
children in the developing world go blind each
year from a deficiency of vitamin A.
Night blindness is one of the first signs of vitamin
A deficiency. Vitamin A deficiency contributes to
blindness by making the cornea
 Vitamin D

Cholecalciferol (D3)
 Vitamin D is a group of fat-soluble
prohormones, the two major forms of which
are vitamin D2 (or ergocalciferol) and vitamin
D3 (or cholecalciferol).[1] The term vitamin D
also refers to metabolites and other analogues
of these substances. Vitamin D3 is produced in
skin exposed to sunlight, specifically
ultraviolet B radiation.
 Forms
Several forms (vitamers) of vitamin D have been
discovered. The two major forms are vitamin D2 or
ergocalciferol, and vitamin D3 or cholecalciferol.
Vitamin D1
Vitamin D2: Vitamin
D3:
Vitamin D4
Vitamin D5
Biochemistry
Vitamin D is a prohormone, meaning that it has no
hormone activity itself, but is converted to the active
hormone 1,25-D through a tightly regulated synthesis
mechanism.
 Nutrition
Only fish is naturally rich in vitamin D, so
much vitamin D intake in the industrialized
world is from fortified products including milk
, soy milk and breakfast cereals or
supplements.
The U.S. Dietary Reference Intake for
adequate intake (AI) of vitamin D for infants,
children and men and women aged 1950 is 5
micrograms/day (200 IU/day)
 Adequate intake increases to 10
micrograms/day (400 IU/day) for men and
women aged 5170 and up to 15
micrograms/day (600 IU/day) past the age of
70. These dose rates will be too low during
winter months above 30 latitude. In the
absence of sun exposure, 1000 IU of
cholecalciferol is required daily for children.
4000 IU of vitamin D may be required for
adults absent summer UVB.
 In food
Natural sources of vitamin D include:
Fish liver oils, such as cod liver oil, 1 Tbs. (15 mL)
provides 1,360 IU
Fatty fish species, such as:
Herring, 85g (3 oz) provides 1383 IU
Catfish, 85g (3 oz) provides 425 IU
Salmon, cooked, 3.5 oz provides 360 IU
Mackerel, cooked, 3.5 oz, 345 IU
Sardines, canned in oil, drained, 1.75 oz, 250 IU
Tuna, canned in oil, 3 oz, 200 IU
Eel, cooked, 3.5 oz, 200 IU
 deficiency
Vitamin D deficiency can result from: inadequate
intake coupled with inadequate sunlight exposure,
disorders that limit its absorption, conditions that
impair conversion of vitamin D into active
metabolites, such as liver or kidney disorders, or,
rarely, by a number of hereditary disorders
Deficiency results in impaired bone mineralization,
and leads to bone softening diseases, rickets in
children and osteomalacia in adults, and possibly
contributes to osteoporosis
including:
 Fish liver oils, such as cod liver oil, 1 Tbs. (15 mL) provides
1,360 IU
Fatty fish species, such as:
Herring, 85g (3 oz) provides 1383 IU

Catfish, 85g (3 oz) provides 425 IU

Salmon, cooked, 3.5 oz provides 360 IU

Mackerel, cooked, 3.5 oz, 345 IU

Sardines, canned in oil, drained, 1.75 oz, 250 IU

Tuna, canned in oil, 3 oz, 200 IU

Eel, cooked, 3.5 oz, 200 IU

 Rickets, a childhood disease characterized by
impeded growth, and deformity, of the long bones.
The earliest sign of subclinical vitamin D deficiency
is Craniotabes, abnormal softening or thinning of the
skull.[
Osteomalacia, a bone-thinning disorder that occurs
exclusively in adults and is characterized by proximal
muscle weakness and bone fragility.
Osteoporosis, a condition characterized by reduced
bone mineral density and increased bone fragility.
 Tocopherol
-Tocopherol
 Tocopherol, a class of chemical compounds of
which many have vitamin E activity, describes
a series of organic compounds consisting of
various methylated phenols. Because the
vitamin activity was first identified in 1936
from a dietary fertility factor in rats, it was
given the name "tocopherol" from the Greek
words [birth], and , [to bear
or carry] meaning in sum "to carry a
pregnancy," with the ending "-ol" signifying
its status as a chemical alcohol.

 Form
Vitamin E exists in eight different forms, four
tocopherols and four tocotrienols. All feature a
chromanol ring, with a hydroxyl group that can
donate a hydrogen atom to reduce free radicals and a
hydrophobic side chain which allows for penetration
into biological membranes. Both the tocopherols and
tocotrienols occur in alpha, beta, gamma and delta
forms, determined by the number of methyl groups
on the chromanol ring. Each form has slightly
different biological activity
 History
During feeding experiments with rats
Herbert McLean Evans concluded in 1922 that besides
vitamins B and C, an unknown vitamin
existed.Although every other nutrition was present, the
rats were not fertile. This condition could be changed
by additional feeding with wheat germ. It took several
years until 1936 when the substance was isolated from
wheat germ and the formula C29H50O2 was
determined. Evans also found that the compound
reacted like an alcohol and concluded that one of the
oxygen atoms was part of an OH (hydroxyl) group
 Sources
Wheat germ oil (215.4 mg/100 g)
Sunflower oil (55.8 mg/100 g)
Almond oil (39.2 mg/100 g)
Hazelnut (26.0 mg/100 g)
Walnut oil (20.0 mg/100 g)
Peanut oil (17.2 mg/100 g)
Olive oil (12.0 mg/100 g)
Peanut (9.0 mg/100 g)
Pollard (2.4 mg/100 g)
Corn (2.0 mg/100 g)
Asparagus (1.5 mg/100 g)
 Deficiency
Vitamin E deficiency causes neurological
problems due to poor nerve conduction. These
include neuromuscular problems such as
spinocerebellar ataxia and myopathies
.Deficiency can also cause anemia, due to
oxidative damage to red blood cells.
 Other uses
Controversy
"Megadoses" of Vitamin E are not recommended
by many government agencies, due to a possible
increased risk of bleeding. A 2005 meta-analysis
by Miller found that high-dosage vitamin E
supplements may increase all-cause mortality.
"High dose" vitamin E esters (>400 units/day)
were also associated with an increased risk in all-
cause mortality of 39 per 10,000 persons, and a
statistically significant relation existed between
dose and mortality, with increased risk at doses
exceeding 150 units per day.
 During pregnancy
Recent studies into the use of both vitamin C
and the single isomer vitamin E esters as
possible help in preventing oxidative stress
leading to pre-eclampsia has failed to show
significant benefits, but did increase the rate of
babies born with a low birthweight in one
study.
 Heart disease
Preliminary research has led to a widely held belief
that vitamin E may help prevent or delay
coronary heart disease, but larger controlled studies
have not shown any benefit. Many researchers
advance the belief that oxidative modification of
LDL-cholesterol (sometimes called "bad" cholesterol)
promotes blockages in coronary arteries that may lead
to atherosclerosis and heart attacks. Vitamin E may
help prevent or delay coronary heart disease by
limiting the oxidation of LDL-cholesterol.
 Vitamin E also may help prevent the formation of
blood clots, which could lead to a heart attack.
Observational studies have associated lower rates of
heart disease with higher vitamin E intake. A study of
approximately 90,000 nurses suggested that the
incidence of heart disease was 30% to 40% lower
among nurses with the highest intake of vitamin E
from diet and supplements. The range of intakes from
both diet and supplements in this group was 21.6 to
1,000 IU (32 to 1,500 mg),
 with the median intake being 208 IU (139 mg).
A 1994 review of 5,133 Finnish men and
women aged 30 - 69 years suggested that
increased dietary intake of vitamin E was
associated with decreased mortality (death)
from heart disease.
 Cancer
Antioxidants such as vitamin E help protect
against the damaging effects of free radicals,
which may contribute to the development of
chronic diseases such as cancer. Vitamin E
also may block the formation of nitrosamines,
which are carcinogens formed in the stomach
from nitrites consumed in the diet. It also may
protect against the development of cancers by
enhancing immune function.
 Vitamin K

This article is about the biomolecule known as

vitamin K. For the unrelated drug sometimes
referred as vitamin K, see ketamine. Vitamin .

Vitamin K1 (phylloquinone). Both contain a

functional naphthoquinone ring and an
aliphatic side chain. Phylloquinone has a
phytyl side chain.
 Vitamin K2 (menaquinone). In menaquinone the side
chain is composed of a varying number of isoprenoid
residues.
Physiology
Vitamin K is involved in the carboxylation of certain
glutamate residues in proteins to form gamma-
carboxyglutamate residues (abbreviated Gla-
residues). The modified residues are situated within
specific protein domains called Gla domains. Gla-
residues are usually involved in binding calcium.
 Blood coagulation : (prothrombin (factor II),
factors VII, IX, X, protein C, protein S and
protein Z ).
At this time 14 human proteins with Gla
domains have been discovered, and they play
key roles in the regulation of three
physiological processes:
Bone metabolism: osteocalcin , also called bone
Gla-protein (BGP), and matrix gla protein
(MGP)
Vascular biology.
 Role in disease
Vitamin K-deficiency may occur by disturbed
intestinal uptake (such as would occur in a
bile duct obstruction), by therapeutic or
accidental intake of vitamin K-antagonists or,
very rarely, by nutritional vitamin K-
deficiency. As a result, Gla-residues are
inadequately formed and the Gla-proteins are
insufficiently active.
 Discovery
In 1929, Danish scientist Henrik Dam investigated
the role of cholesterol by feeding chickens a
cholesterol-depleted diet. After several weeks, the
animals developed hemorrhages and started bleeding.
These defects could not be restored by adding
purified cholesterol to the diet. It appeared that -
together with the cholesterol
 a second compound had been extracted from
the food, and this compound was called the
coagulation vitamin. The new vitamin received
the letter K because the initial discoveries
were reported in a German journal, in which it
was designated as Koagulationsvitamin.
Edward Adelbert Doisy of
 Saint Louis University did much of the
research that led to the discovery of the
structure and chemical nature of Vitamin
K.Dam and Doisy shared the 1943 Nobel Prize
for medicine for their work on Vitamin K.
Several laboratories synthesized the compound
in 1939.

Mineral
A mineral is a naturally occurring substance
formed through geological processes that has a
characteristic chemical composition, a highly
ordered atomic structure and specific physical
properties. A rock, by comparison, is an
 aggregate of minerals and need not have a
specific chemical composition. Minerals range
in composition from pure elements and simple
salts to very complex silicates with thousands
of known forms. The study of minerals is
called mineralogy.
 Mineral definition and classification
To be classified as a true mineral, a substance
must be a solid and have a crystalline
structure. It must also be a naturally occurring,
homogeneous substance with a defined
chemical composition. Traditional definitions
excluded organically derived material.
However, the
International Mineralogical Association in
1995 adopted a new definition:
 a mineral is an element or chemical compound
that is normally crystalline and that has been
formed as a result of geological processes.
The chemical composition may vary between
end members of a mineral system. For example
the plagioclase feldspars comprise a continuous
series from sodium-rich albite (NaAlSi3O8) to
 calcium-rich anorthite (CaAl2Si2O8) with four
recognized intermediate compositions
between. Mineral-like substances that don't
strictly meet the definition are sometimes
classified as mineraloids. Other natural-
occurring substances are nonminerals.
Industrial minerals is a market term and refers
to commercially valuable mined materials (see
also Minerals and Rocks section below).
 Physical properties of minerals

Classifying minerals can range from simple to

very difficult. A mineral can be identified by
several physical properties, some of them being
sufficient for full identification without
equivocation. In other cases, minerals can only
be classified by more complex chemical or
X-ray diffraction analysis; these methods,
however, can be costly and time-consuming.
 Physical properties commonly used are:
Crystal structure and habit: See the above
discussion of crystal structure. A mineral may
show good crystal habit or form, or it may be
massive, granular or compact with only
microscopically visible crystals.
 Talc
Rough diamond.
Hardness: the physical hardness of a mineral is
usually measured according to the Mohs scale.
This scale is relative and goes from 1 to 10.
Minerals with a given Mohs hardness can
scratch the surface of any mineral that has a
lower hardness than itself.
 Talc Mg3Si4O10(OH)2
Gypsum CaSO42H2O
Calcite CaCO3
Fluorite CaF2
Apatite Ca5(PO4)3(OH,Cl,F)
Orthoclase KAlSi3O8
Quartz SiO2
Topaz Al2SiO4(OH,F)2
Corundum Al2O3
Diamond C (pure carbon)
Lustre
 Color indicates the appearance of the mineral
in reflected light or transmitted light for
translucent minerals (i.e. what it looks like to
the naked eye).
Streak refers to the color of the powder a
mineral leaves after rubbing it on an unglazed
porcelain streak plate
 Note that this is not always the same color as
the original mineral.
Cleavage describes the way a mineral may
split apart along various planes. In thin
sections, cleavage is visible as thin parallel
lines across a mineral.
 Fracture describes how a mineral breaks when
broken contrary to its natural cleavage planes.
Chonchoidal fracture is a smooth curved fracture
with concentric ridges of the type shown by glass.
Hackley is jagged fracture with sharp edges.
Fibrous
Irregular
 Chemical properties of minerals
Minerals may be classified according to
chemical composition. They are here
categorized by anion group. The list below is
in approximate order of their abundance in the
Earth's crust. The list follows the Dana
classification system.
 Silicate class
quartz
The largest group of minerals by far are the
silicates (most rocks are 95% silicates),
which are composed largely of silicon and
oxygen, with the addition of ions such as
aluminium, magnesium, iron, and calcium.
Some important rock-forming silicates include
the feldspars, quartz, olivines, pyroxenes,
amphiboles, garnets, and micas.
 Carbonate class
The carbonate minerals consist of those
minerals containing the anion (CO3)2- and
include calcite and aragonite dolomite and
siderite . Carbonates are commonly deposited
in marine settings when the shells of dead
planktonic life settle and accumulate on the
sea floor.
 Carbonates are also found in evaporitic
settings and also in karst regions, where the
dissolution and reprecipitation of carbonates
leads to the formation of caves, stalactites and
stalagmites. The carbonate class also includes
the nitrate and borate minerals.
 Sulfate class
Sulfates all contain the sulfate anion, SO42-. Sulfates
commonly form in evaporitic settings where highly
saline waters slowly evaporate, allowing the
formation of both sulfates and halides at the water-
sediment interface. Sulfates also occur in
hydrothermal vein systems as gangue minerals along
with sulfide ore minerals. Another occurrence is as
secondary oxidation products of original sulfide
minerals
 Halide class
Halite
The halides are the group of minerals forming
the natural salts and include fluorite (calcium
fluoride), halite (sodium chloride), sylvite
(potassium chloride), and sal ammoniac
(ammonium chloride). Halides, like sulfates,
are commonly
 found in evaporitic settings such as playa lakes
and landlocked seas such as the Dead Sea and
Great Salt Lake. The halide class includes the
fluoride, chloride, bromide and iodide
minerals.
 Oxide class
Oxides are extremely important in mining
as they form many of the ores from which
valuable metals can be extracted. They also
carry the best record of changes in the
Earth's magnetic field. They commonly
occur as precipitates close to the Earth's
surface, oxidation products of other
minerals in the near surface weathering
zone, and as accessory minerals in igneous
rocks of the crust and mantle.
 Common oxides include hematite (iron oxide),
magnetite (iron oxide), chromite (iron
chromium oxide), spinel (magnesium
aluminium oxide - a common component of
the mantle), ilmenite (iron titanium oxide),
rutile (titanium dioxide), and ice (hydrogen
oxide). The oxide class includes the oxide and
the hydroxide minerals.
 Phosphate class
The phosphate mineral group actually includes any
mineral with a tetrahedral unit AO4 where A can be
phosphorus, antimony, arsenic or vanadium. By far
the most common phosphate is apatite which is an
important biological mineral found in teeth and bones
of many animals. The phosphate class includes the
phosphate, arsenate, vanadate, and antimonate
minerals.
 Element class
The elemental group includes metals and
intermetallic elements (gold, silver, copper), semi-
metals and non-metals (antimony, bismuth, graphite,
sulfur). This group also includes natural alloys, such
as electrum (a natural alloy of gold and silver),
phosphides, silicides, nitrides and carbides (which are
usually only found naturally in a few rare meteorites).
 Organic class
The organic mineral class includes biogenic
substances in which geological processes have been a
part of the genesis or origin of the existing
compound. Minerals of the organic class include
various oxalates, mellitates, citrates, cyanates,
acetates, formates, hydrocarbons and other
miscellaneous species. Examples include whewellite,
moolooite, mellite, fichtelite, carpathite, evenkite and
abelsonite.
 Carbohydrate is generally defined as a neutral
compound made up of carbon, hydrogen and oxygen,
the last two elements remaining in the same proportion as in
water. The general formula is cn (H2 O) . But there are many
exceptions. For instance, rhamnose (C6 H12 O5 ) is a
carbohydrate in which H and O remain in a different
proportion. Also there are certain other compounds, such as
formaldehyde (HCHO), acetic acid (CH3COOH),lactic acid
(CH3CHOHCOOH), etc., which have got the same empirical
formula but are not carbohydrates. Thus chemically,
carbohydrates can be defined as the aldehyde and ketone
derivatives of higher polhydric alcohol (having more than OH
group).
 Carbohydrate are classified according to the
number of simple sugar units present in
the molecules, viz.

(1) Simple carbohydrates.

(2) Compound carbohydrates.

I. SIMPLE CARBOHYDRATES OR MONOSACCHARIDES

OR SIMPLE SUGARS.
 They contain only one unit of simple sugar. For
instance, glucose, fructose, galactose, etc.
Monosaccharide are further subdivided in two ways.
(1) According to the number of carbon atoms presents
in the molecules, viz., 1,2,3,4,5,6 and 7 carbon
atoms respectively.
(2) According to the nature of the reducing group they
contain, viz.
(a) Aldoses, e.g., glucose. Here, the reducing
group is an aldehyde (-CHO) radicle.
(b) Ketoses- these contain ketone (C=O) group,
viz. fructose. The general formula of
monosaccharide is Cn(H2O)n.
 They are colour crystalline compound having a taste
Chemically they are derivatives of polyhydric alcohols. The
aldoses are derived from primary alcohols and the ketoses
from secondary alcohols
Formation of esters. By virtue of the alcohol group they easily
from esters with acid, eg., acetates, benzoates , etc. Sach
esters, having great physiological importance, are those of
phosphoric acid , viz., hexose phosphates, which play an
important role in carbohydrat metabolism;
pentose phosphates, present in the nucleic acid and such
others.
 Reducing power By virtue of the aldehyde (_CHO) or
(C=O) group , simple sugars are powerful reducing agents.
They easily reduce alkaline copper , bismuth or silver
solutions.
Isomerism . Due to presence of asymmetric carbon atom in
the molecule , monosaccharides may remain in different
isomeric forms.
Optical rotation . Simple sugars rotate the plane of polarised
light and therefore may exist in either dextro or laevo forms.
 Condensation . Simple sugars condense and from bigger carbohydrate
molecules, viz., polysaccharides.
Formation of glycosides. When replaceable hydrogen atom of a
hydroxyl group from sugar is substituted with other radicles it is
called a glycoside; that formed from glucose is a glucoside, from
galactose a galactoside and the like . A good number of glycosides
occur in leaves, roots, etc., of plants and are bitter solids, Phlorizine
(glucose + phloretin ), digitonin (galactose + xylose + digitogenin ),
indican (glucose + indoxyl )are a few examples of them .
Sugar acids , Either carbon atom one or six in a hexose molecule may
be oxidised to carboxyl group That formed from oxidation of number
one is named hexonic acid (glucose --> gluconic acid ), and from six
called uronic acid (glucose --> glucuronic acid ) . Many drugs and a
number of hormones combine with glucuronic acid in the body and
are excreted as glucuronides.
 Formation of hexosamine . Replacement of hydroxyl group in hexose
sugar with amino one produces amino sugar or hexosamine, that
formed from glucose is glucosamine . They occur in some complex
polysaccharides.
Osazone formation . All reducing sugars condense with
phenylhydrazine and produces osazone compounds. The crystalline
forms of these osazone compounds are so characteristic that they can
be used for the identification of the particular sugar . However
glucose, glucosamine and fructose from similar osazones.
Ring Structures of the sugars, sugars not only remain as straight chain
compounds but may also remain in the form of rings , This ring may
include six members or five members Haworth has suggested all
sugars having six membered rings to be called pyranoses and those
forming five membered ring , furanoses.

 A second important group of organic compounds in lipids

(lip = fat). Lipids make up 18-25% of body mass in leanadults. Like
carbohydrates, lipids contain carbon, hydrogn, and oxygen. Unlike
carbohydrates, they do not have a 2:1 ratio of hydrogen to oxygen.
The proportion of electronegative oxygen atoms in lipids is usually
smaller than in carbohydrates, so there are fewer polar covalent
bonds. As a results, most lipids are insoluble in polar solvents such
as water; they are hydrophobic. Nonpolar solvents such as
chloroform and ether, however, readily dissolve lipids. Because they
are hydrophobic, only the smallest lipids (some fatty acids) can
dissolve in watery blood plasma. To become more soluble in blood
plasma, other lipid molecules form complexes with hydrophilic
protein molecules. The resulting lipid and protein particles are
termed lipoproteins.
 The diverse lipid family includes triglycerides (fats and
oils), phospholipids (lipids that contain phosphorus), steroids
(lipids that contain rings of carbon atoms), eicosanoids (20-
carbon lipids), and a variety of other lipids, including fatty
acids, fat-soluble vitamins (vitamins A,D, E, and k), and
lipoproteins. introduces the various types of lipids and
highlights their roles in the human body.
 Types of Lipids in the Body

Type of Lipid
Triglycerides (fats and oil)

Phopholipids
Function
Protection, insulation, energy, Storage.
Steroids.
Cholesterol

Bile salts

Vitamin D

Adrenocortical hormones

Sex hormones

Eicosanoids
Major lipid component of cell membranes.

Minor component of all animal Cell

membranes; precursor of bile salts, vitamin D, and steroid hormones.
Needed for a absorption of dietary lipids.
Helps regulate calcium level in the body; needed for bone growth and repair.
Help regulate metabolism, resistance to stress, and salt and water balance.

Stimulate reproductive functions and sexual characteristics.

Have diverse effects on blood clotting, inflammation, immunity, stomach acid secretion, airway
diameter, lipid breakdown, and smooth muscle contraction.
 Types of Lipids in the Body

Type of Lipid Functions

Other Lipids
Fatty acids

Carotenes Catabolized to generate adenosine triphosphate (ATP) or used to

synthesize triglycerides and phospholipids.
Vitamin E
Needed for synthesis of vitamin A, which is used to make visual
pigments in the eyes.
Vitamin K

Promotes wound healing prevents tissue scarring contributes to the

Lipoproteins normal structure and function of the nervous system and functions
as an antioxidant.

Required for synthesis of bloodclotting proteins.

Transport lipids in the blood, carry triglycerides and cholesterol to

tissues and remove excess cholesterol from the blood.
 LIPIDS AND FATS

Lipids are defined to be the esters of higher aliphatic acids with a characteristic property of
insolubility in water and solubility in fat solvents like chloroform ,ether, benzene and carbon
tetrachloride, Due to the presence of replaceable OH group, alcohol behave like alkalies and as
such, combine with acids, forming salts and H 2O. These salts of alcohol with acid are technically
known as esters.
They may be represented thus (HOOC- F represents fatty acids).

CH2 OH H O.OC-F CH2O.OC-F

CH OH H O.OC-F CHO.OC-F + 3H2O

CH2 OH H O.OC-F CH2.O.OC-F

Glycerol Fatty acids Mixed triglyerids water

 Fatty acid esters may be formed with alcohols other than glvcerol, such as waxes. The
commonest types of fatty acids occurring in natural fats usually contain even number of
carbon atoms and are strainght chain derivatives. They may be saturated or unsaturated.
Saturated fatty acids do not contain double bonds, but unsatrurated fatty acids contain one or
more double bonds or ethylenic groups. The general formula of fatty acids is C nH2n+1COOH.

The common saturated fatty acids are :

(a) butyric acid (C3H7COOH),
(B) palmitic acid (CH3(CH2)14 COOH),
(C) stearic acid (CH3(OH2)18 COOH).
The unsaturated fatty acids are :
(a) oleic acid (CH3 (CH2)7 CH = CH(CH2)7 COOH) with one double bond,
(b) crotonic acid (CH3-CH = CH COOH),
(c) linoleic acid (C17H31COOH)
(d) linolenic acid (C17H29COOH)
Classification of Lipids
Lipids are classified in (1) simple lipids, (2) compound lipids, (3) sterols
or steroids, (4) Hydrocarbons.

1) Simple Lipids
i) True Fats :- These are esters of fatty acids with glycerol (CH2-OH-
CHOH-CH2OH) and are generally called triglycerides. On hydrolysis
with water at high temperature and pressure in an autoclave in the
presence of acids, triglyceride may yield three molecules of fatty
acids and

H2C-O-CO-C17H35 H2C-O-CO-C17H33
HC-O-CO-C17H35 HC-O-CO-C17H35

H2C-O-CO-C17H35 H2C-O-CO-C15H31
Simple glycerides Mixed glycerides
One molecule of glycerol, Furthermore, if the rriglycerides are boiled
with alkali, such as NaOH or KOH then glycerol and Na or K salt of
fatty acids (soap) are formed Triglycerides having unsaturated fatty
acids may
H2C-O-CO-C17H35+KOH H2COH

HC-O-CO-C17H35+KOH HCOH
3C17H35COOK
+
H2C-O-CO-C17H35+KOH H2COH
Soap(Potassium
Stearin
stearate)
Glycerol

Be hydrogenated at their double bonds in the presence of nickel

catalyst. Commercial cooking fats are mostly hydrogenated fats
and becomes hard due to hydrogenation.
2. Waxes :- These are esters of fatty acids with alcohol
other than glycerol. In the human body most abundant In the
blood, suprarenal glands, the gonads and the sebaceous glands
of the skin. Like true fats, the natural waxes are also complex
mixtures. They are solid at ordinary temperature and are not so
readily hydrolysed as fats.
II) Compound Lipids

Fats combined with other non-fatty prosthetic groups.

1. Phospholipids or Phosphatids :- (Fats containing phosphoric

acid and a nitrogenous base in the molecule) So far three types
of phosphatids habe been identified. (a) Lecithin It is composed
of 1 molecule of
CH2O.CO.R1
glycerol I Fatty acids
CHO.CO.R2
I
CH2O-P-O-CH2CH2
It occurs in two forms- -lecithin
\\ and lecithin
O N (CH3)3

OH HO

Phosphoric acid Choline

-Lecithin
Glycerol, 2 molecules of fatty acids and I molecule of phosphoric
acid. Another nitrogenous base (choline) remains attached to the
phosphoric acid. When placed in water it swells up and readily
forms an embulsion. Due to presence of acid and basic groups, it
combines both with bases and acid. Its is a pale-yellow solid which
readily absorbs water and oxygen when exposed to air and light
and is thus transformed into a dark-plastic mass. (b) Kephalin
(Cephalin). Its is similar to lecithin except that instead.

CH2-O-CO -R

R-CO-O-CH O
II
CH2-O-P-O-CH2-CH2
I
O- NH3 +
-kephalin(zwitlerion form)
Of choline the nitrogenous base here, is ethanolamine. It
occurs in two forms. Kephalin and Kephalin. Kephalin
and lecithin occurs together in the tissue and their
properties are generally similar. Howell claims that the
substance thrombokinase which initiates blood clotting is
identical with Kephalin. It is found specially in nerve tissues,
egg-yolk, milk, etc. (c) Sphingomyelin. Its constituents are
same as lecithin except that glycerol is replaced by another
unsaturated nitrogenous alcohol called sphingosine. It is

HO NH2
OH

CH3(CH2)12 CH = CH CH CH
CH2
Sphingestiar

Stable is light and air, and is a white crystalline solid. It is

also found in the animal tissues specially in nerve tissues,
egg-yolk, milk, etc. Due to the
 O
II
- O P O CH2 CH2 N+ - (CH3)3
I
HO O

CH3(CH2)12 CH = CH CH CH CH2
I
NH
I
C=O
I
R
Sphigomyelin
Presence of two asymmetric carbon atoms, 4 stereo-isomers are possible . The natural
forins are dextrorotatory, (d) Plasmalogen. It is another type
CH2 O CH = CH R
I
CH O CO R
I OH
I
CH2 O P - O CH2 CH2 NH2
II
O
Phosphatidal ethanolamin plasmalogen
Of phospholipid present in the brain, liver and muscle tissue. After
hydrolysis it vields cholmine esters of - and -glycerophosphoric adic
along with a mixture of higher aldehyde. Both palmitic and stearic
aidehydes have been found to be the constituents of plasmalogon.
2. Glycolipids (Cerebrosides) :- In general properties they
resemble the sphingomyelins. It is also named as glycosphingosides.
They are specially abundant in the brain. They are characterised by the
presence of galactose in the molecule. For this reason they are also
called galactolipids. Three cerebrosides have been identified, e. g. ,
phrenosin, kerasin and nervon. The existence of another member of this
class oxynervon, has also been suggested. They all contain fatty acids,
galactose and the nitrogenous base sphingosine. The difference
between cerebrosides is due to
 HO H

CH3(CH2)12 CH = CH CH CH CH2 O C

HN HCOH

CO HOCH

O
R HOCH

HC

CH2OH

Glycolipid or glycosphingoside or Cerebroside

The difference in fatty acids. The function of cerebrosides is not known
as yet.

3. Gangliosides :- They contain sphingosine, fatty acid, hexose

hexose-amine and sialic acid. Gangaliosides have been found in
nerve cells and also in spleen and red blood cells. In niemamm-Pick
disease a large amount of them are present in brain.

4. Lipoproteins :- Protein molecules conjugated with neutral fats

(triglycerides), cholesterol or phospholipids, e. g. , - and -
lipoprotein in plasma. Changes in one or other fraction have been
noted in coronary disease, in acidosis accompanying diabetes, in
essential hyperlipaemia, etc. Lipoprotein is also present in cell
membrance, milk, egg-yolk, etc.

5. Sulpholipids :- They are sulphuric ester of sphingosine cerebronic

acid and galactose (cerebron). Largest amount has been observe in
white matter of brain and to a lesser extent in liver, kidney, salivary
gland, testis, etc.
III. STEROIDS OF STEROLS

Chemistry :- Steroids or sterols are not true fats. Steroids are

derivatives of phenanthfence and have the parent nucleus
(perhydrocyclopentanophenanthrence) with 17 carbon atoms
consistings In 3 hexagon and I pentagon rings and hydrogen atoms
are added until the valency reaches 4. When the natural steroids
have a methyl group at C 13 and generally at C 10 and possess
one or more alcoholic groups, then these secondary alcohols are
sterols. Steroids are found free or in ester bonds with fatty acids
(cholesterides) and can be extracted by organic solvents along with
fats. Cholesterol, coprosterol, ergoserol, male and female sex
hormones, adrenocortical hormones and vitamin D are major
steroids.
 CH2 CH2
12 17

H2CII CH
13 CH2
16

H2C HC 14 HC 15 CH2
1 9

H2C2 HG10 CH
3

H2C3 CH
5 CH2
7

4 6

H2C CH2

Distribution :- Sterols are widely distributed in both animal and

vegetable kingdoms. In the plants they exist chiefly as phytosterols.
In the animals they are present in all cells, both in the cell
membreance as wel as in the cytoplasm. They always remain along
with phospholipids. They are found both as free sterols as well as
sterides.
Synthesis, Destruction and Excretion :- Sterols can be synthesised in the
body from non-sterol sources. It has been definitely proved in the case of
cholesterol. The body can destroy sterols to some extent but the power is
very limited.

Cholesterol
Chemistry and Properties :- It is a complex monohydric secondary
alcohol being a very Important member of sterol class. With Fatty acids it
forms waxes. It is a stable white crystalline substance, insolublc in water
but readily soluble in chloroform, either, alcohol and other fat solvents.
The crystals have a rhombic or rectangular shape, with one corner
broken off. Cholesterol when mixed with fats or oils helps them to absorb
a large volume of water due to formation of water in oil emulsion.
 CH2

H 2C HC CH

CH2
CH3
CH2
H2C C
CH2 CH2

H 2C HC HC H2C - CH
CH2
CH2
CH3
H 2C C CH

HC C CH2

HO H2C HC
Distribution :- The broad facts about the distribution of cholesterol are
given below.
1) It is present In all cells both in the cell membrance and cytoplasm.
2) All body fluids contain cholesterol, excepting cerebrospinal flurid in
which the
amount is negligible.
3) It may exist in the free state as well as in the form of esters, but these
two forms are not equally distributed every where. In bile it is present
only in the free forms.
4) Brain (17%) and suprarenals have the richest supply. In the former it
is found mainly in the free form.
5) Blood cholesterol. Normal blood cholesterol varies between 0.15 % to
0.2 %. The total quantity is equally distributed between plasma and
corpuscles. But in the corpuscles it is present chiefly in the free form,
while in the plasma the major part remains as esters.
6) The free cholesterol content of a tissue is characteristic and normally
remains very constant but the cholesterol esters may very in amount.
Interrelation with other Sterols :- Cholesterol is very closely
related to
many others sterols of immense physiological importance, for instance
(a) The active principles of adrenal cortex, (b) the male sex hormones, (c)
 IV - HYDROCARBONS
Hydrocarbons are the substances which have got no structural
relationship to fatty acids but yet they are grouped as lipids only because
of their similar solubility properties. These are squalene, carotenes,
vitamins A, E and K.
PROPERTIES OF LIPIDS
(a) PHYSICAL :
1. Solubility : They are insoluble in water but solible in ether,
chloroform, benzene, petroleum-ether, carbon fetravcholride, hot alcohol,
etc. (true fats are colourless, odourless and tasteless.)
2. Consistency : At ordinary temperature, some fats remain solid
whereas others in liquid forms. Unsaturated fats are generally liquid.
Those fats which remain liquid at ordinary temprature are called oils.
3. Melting Points : Different fats have different melting points. For
instance pure tristearin melts at 71.5oC; beef fat melts at 49.5C ; human
fat at 17C.; Glycerides of unsaturated fatty acids have lower melting
points than those of saturned fatty acids.
4. Specific Gravity. It is less than 1.0, i.e., lighter than water. Solid fats
are lighter than the liquid fats.
5. Spreading & Surface Tension. When liquid fat as poured on water, it
spreads uniformly over the surface in a unimolecular layer & reduces the
surface tension of water.
(b)CHEMICAL :
1. Reaction. True fat is neutral in reaction and colourless, but after
exposure to air it becomes acid in reaction & yellow in colour owing to
partial hydrolysis of fats and oxidation of the unsaturated fatty acids.
When thus altered, the fat is said to become rancid. Antioxidants
present in natural fats prevent this rancidity to some extent.
2. Hydrolysis. By boiling with acids or alkalies or by applying
superheated steam, fats can be completely hydrolysed into fatty
acids and glycerol.
3. Saponification number (value). When fats are boiled with alkali,
soaps are formed and the process is termed saponification. In this
way Na, K, Ca, Mg, Li, soaps are formed by boiling fats with
corresponding hydroxides, By the term saponification number
(saponification value) of fat is meant the amount of potassium
hydroxide (KOH) is mg required to saponify completely 1 gm of fat.
4. Addition Reactions. Fats contaning unsaturated fatty acids can take
up other elements and thus become saturated. Two such addition
reaction are of physiological interecst. (a) Iodine number Under
suitable conditions double bonds of unsaturated fatty acids may be
made to take up halogens, bromine or iodine. By the term iodine
number (regardless of up halogens, used) of fat, is meant the number
 Hydrogenatin just like iodine, an unsaturated fat may be made to
take yo hydrogen atoms in the presence of a catalyst, especially
nickel. For instance, addition of two H atoms to oleic acid would give
the corresponding sturated acids.

5. Oxidation. Unsaturned fatty acids when exposed to air are easily

oxidised to form various aldehydes and ketones, which may react
further and form complex resinous compounds. For this reason,
linseed oil when spread in a thin layer, is rapidly converted A tough
waterproff film which adheres closely uponthe surface.
6. Acetyl number. It is defined as the mgs of KOH required to combime
with the acetic acetic liberated by the saponification of 1gm of
acetylated fat.
7. Rancidity. It is a chemical change that may results unpleasant odour
and taste within the natural fat due to keeping for long time. This is due
to hydrolysis of fat into free fatty acids and glycerol or mono and di-
glycerides. Acid number determines the rancidity or free fatty acids
present in the fat. It is defined as mgs of KOH is required to neutralise
the free fatty acids present in 1 gm of fat.
8. Reichert-Meissl number or volatile acid value. It is ml of 0.1 normal
(N) KOH required to neutralise evolatile fatty acids obtained during
distillation of 5 gm of hydrolised fat after it has been saponified with
KOH and then made acid with H3PO4 or H2SO4 This value actually
determines the presence of total fatty acids of low molecular weight.
Functions of lipids. (a) Food material : Lipid provides a food
with a high
calorific value (1 gm produces about 9.3 kilocaloris of heat. (b) Food
reserve : Lipid acts as reserved food materials, because it is readily
stored in the body on account of its insolubility in aquesous solutions.
(c) Heat insulation : Being deposited in subcutaneous tissue lipid acts
as an insulator. Subscutanrous fat contents are higher in aquatic
animal (i.e., whale) and in animals living in cold climates. (d) Solvents :
lipid acts as vehicle of natural fat-soluble vitamins A,D and E .
(e) Structural Consituent : Lipid is a structural component of
the cell membrane. (f) Fat transport : Phospholipids play an
important role in absorption and transportation of fatty acids.
(g) Hormone synthesis : Adrenocorticoids sex hormones,
vitamin D and cholic acids are synthesised from cholestrol
 Fermentation. Sugar , in general undergo fermentation by yeast and
other micro organisms.

(1). Trioses. Two trioses are of great physiological
importance glyceric aldehyde and dihydroxyacetone. The
corresponding phosphoric acid esters phosphoglyceraldehyde
and dihydroxyacetone phosphate are of great physiological
value.
 (2) . Pentoses.
(a) Two different pentoses are present in two nucleic acids RNA.
Sugar ribose is present in the RNA, where as that present in DNA is
deoxyribose. In the free state both the sugars exist in the pyranose
form. In combination with nucleic acids they exist as
deoxyribofuranose and ribofuranose.

(b) Arabinose __-It is also pentose commonly found in gum arabic-

chiefly as l-arabopyranose.

(3). Hexoses The following hexoses are of physiological
importance.
a. Glucose . It is found in grapes, dextrorotatory and is an aldose.
Glucose is found in nature in free from , in the from of disaccharides,
in the from of polysaccharides and in combination with proteins . It
may remain both as a straight chain compound and as well as, in
various ring forms . a- and b- glucose are the isomeric forms.
 The optical reaction of glucose is peculiar . As soon as dextrose is
dissolved in water it gives a specific rotation of +112 . On standing
the rotation gradually diminishes and finally remains constant at
+52.5 .this phenomenon is called mutarotation. If however, dextrose
be first recrystallised from boiling pyridine, its solution in water at
first gives a rotation of +19 and not +112. This solution on standing
also shows mutarotation in which the specific rotation gradually
increases and finally becomes constant at the same value, +52.5 .
This shows that when in solution one particular variety changes into
the other, until an equilibrium mixture of the two forms is produced
with a constant rotation of +52.5 . Due to asymmetrical nature of
carbon atom 1 in ring form of glucose , it can exist in two forms. The
a-glucose has a rotation of =112 and the B-form , +19. A solution of
glucose is an equilibrium mixture between the straight chain and both
a- and B-ring forms, the percentage of B- being more than a- Glucose
forms esters with phosphoric acid.
 b. Fructose
It is laevorotatory and is a ketone. Free fructose is present in honey
and nearly in all sweet fruits in combination it cane sugar and insulin.
In the human body normally it does not occur in free state and rapidly
converted into glucose in the liver and intestine. In contrast with other
sugars, fructose is soluble in hot absolute alcohol . Like glucose it also
forms phosphoric acid esters which play an important role in
carbohydrate metabolism.
 c. Glucose . It does not occur free in nature. In the body it is
found as a constituent of lactose and cerebrosides . As polysaccharide
it is present in lichens, mosses, sea-weeds,etc
 d. Mannose does not occur free in nature . It is found as a
constituent of certain animal proteins and converted to glucose in the
body. It is also found as a polysaccharide known as mannan specially
found in the ivorynuts.

(4) . Heptoses.
In the metabolic pathway of pentose phosphate by hexose
monophosphate shunt, a seven carbon ketosugar, sedoheptulose is
formed as an ester with phosphoric acid ,
 2.Compound Carbohydrates
These are made up of from two to one thousand or more than
thousand monosaccharide units either with or without non
carbohydrate units. Thus on hydrolysis these may give rise to
monosaccharide and non-carbohydrate units. These are
principally of two type;

(a) Simpler Compound

(b) More Complex Compound
 The Simpler Compound carbohydrate contains only a few
monosaccharide units and are crystalline, water soluble and given
sweet taste . These simpler compounds are generally called
Oligosaccharides. Oligosaccharides on hydrolysis give rise to at least
two to ten monosaccharide units. Thus oligosaccharides are composed
of Disaccharides , Trisaccharides and Tetrasaccharides ,

More Complex Compounds -- these carbohydrates include

glycogen , cellulose, starch and also dextrin's which are composed of
ten or more monosaccharide units . These are mostly tasteless and are
amorphous solid substance , As these compounds are composed of
many monosaccharide units, these are called polysaccharide which
are composed of ten or more monosaccharide units, held together by
glycosidic linkages. Those polysaccharides are composed of
monosaccharides are called Homoglycans whereas those are made up
of two or more different types of monosaccharides are named as
hetroglycans..
 Simpler Compound Carbohydrates
Oligosaccharides - include

(a) Disaccharides,

(b) Trisaccharides,

(c) Tetrasaccharides,
 Disaccharides
These can be regarded as condensation products of two monosaccharide
units with the elimination of one molecule of water. Their general
formula is C (H O) During union the active groups become
engaged. In lactose only one aldehyde group becomes engaged and
one aldehyde group remains free. Similar is the case with maltose. But
in case sugar both the active radicles (--CHO of glucose and CO of
fructose) become engaged. For this reason lactose and maltose can
reduce alkaline copper , form any osazone crystals and exhibit
mutarotation . Cane sugar , on the other hand, in which both the active
radicles are engaged, shows no reducing power, dos not form any
osazone nor shows any mutarotation . In nature about 16
disaccharides are present . Of these only the following three are of
physiological importance.
 Lactose (milk sugar)
composed of one molecule of glucose and one of galactose, found in
the milk of mammals.
 Maltose (Malt sugar)
composed of two glucose units , it is an intermediate product in
digestion of starch.
 Sucrose (Cane sugar)
On hydrolysis it gives rise to one molecule of glucose and one of
fructose. It is the chief form of sugar taken in diet. It is widely
distributed in many plants juices, such as sugar cane , sugar maple,
pine apple and also in sugar beets. Sucrose is dextrorotatory but on
hydrolysis the resulting mixture becomes laevorotatory owing to the
liberation of fructose. The laevo rotation of fructose is greater then the
dextro rotation of glucose. For this reason the mixture is known as
invert sugar and the enzyme which hydrolyses sucrose is also called
invertase .
 Trehalose
it is present in the haemolymph of insects as the principal sugar, also
occurs in yeast and fungi.
 A
S
I
These type of oligosaccharides on hydrolysis give rise to three
monosaccharides units. These trisaccharides are:
R
T
(1) Mannotriose
giving rise to two molecules of galactose and
one molecules of glucose on hydrolysis.
(2) Robinose--
on hydrolysis gives rise to galactose and two
molecules of rhamnose.
(3) Rhamninose
on hydrolysis gives rise to galactose and two
molecules of rhamnos.
 (4) Raffinose
onhydrolysis gives rise to fructose , glucose and
galactose .
(5) Gentianose
on hydrolysis gives rise to fructose and two
molecules of glucose
(6) Melibiose
On hydrolysis give rise to fructose and two
molecules of glucose. Among six trisaccharides described, the first
three are reducing and rest three are non-reducing the general formula
of trisaccharides is C (H O)
 Only two tetrasaccharides are known. These are
(1) Stachyose which is composed of Dglucose, --galactose and
fructose found in stachys tuberifera and

(2) Scorodose in the bulbs of garlic and onion,

 Polysaccharides are made up of a large number of monosaccharide
units. During condensation all the active radicles become engaged, so
that they do not show any reducing power, do not produce any
osazone and are generally not sweet to taste. They are soluble in water
excepting cellulose. The molecules are large and hence, show
colloidal properties. The empirical formula of polysaccharides is (C
H O).
Polysaccharides are classified according to the nature of the
constituent units . For instance, those made up of pentose units are
called pentosans, those of hexose units hexosans,etc. More
specifically they are composed. For instance, glucosans are made of
glucose, galactans of galactos, fructosans of fructose and such other.
 Starch, glycogen and cellulose are glucosans. Inulin is a fructosan.
Agar agar is a galactosan Gums are mixtures of both pentosans and
hexosans.

Starch.
This is the chief form of carbohydrate taken in diet. It is
manufactured by the plants and plays the same role in them as
glycogen dose in animals, I.e., an easily available sugar store. It is the
main constituent of food grains. Starch form different sources can be
identified form their microscopic peculiarities . It is insoluble in cold
Water due to the presence of an outer cellulose layer around the
granule. On boiling the insoluble cellulose covering ruptures and
starch enters into a colloidal solution. It is a glucosen and on
hydrolysis breaks down into glucose. It gives blue colour with iodine .
It has got no reducing power and is tasteless. Starch is a mixture of
two substance having similar structure amylose (mol wt 60.000)
 And amylopectin (mol. Wt.300.000) both being composed of chains of
24 to30 glucopyranose units.

Glycogen.
it is called animal starch ; because it is in this form
that glucose remains stored in the liver and muscles of animal body.
Glycogen is also found in those plants which do not possess any
chlorophyll, such as yeast, fungi, etc., but not in green plants. There is
probably more than one type of glycogen. When rabbit is fed with
glucose , it synthesises a glycogen containing 12 glucose units, but if
fed with galactose it forms a glycogen with 18 glucose units , but
curiously enough , mixtures of glycogens with 12 and 18 units .are not
found. Glycogen is soluble in water, makes an opalescent solution and
gives reddish colour with iodine. The glycogen molecule contains
many glucose units. The units are joined by linkage between carbon 1
of one unit to carbon 4 of the next one; branches involving 1,6
linkages are frequently present.
 (c) Dextrins
They do not occur naturally, but are the split
products of starch resulting form hydrolysis For this reason they ought
to have been described as derived carbohydrates. The term dextrin is a
group name including several varieties of dextrins. The earlier
products of hydrolysis of starch all called dextrins the name of the
different dextrins are given according to their colour reaction with
iodine. The first dextrin formed is amylodextrin giving blue colour
with iodine, the next product is called erythrodextrin giving red colour
with iodine and the next product gives no colour with iodine and is
called achroodextrin. As these products become smaller and smaller,
they develop more and more the characteristic properties of
monosaccharide, such as the reducing power, a sweet taste and the
others.
 (d) Cellulose.
it is a stable, insoluble compound, found in the
plants and never present in the animal body. Cellulose is taken with
vegetable food. It can not be digested by the human beings .
Herbivorous animals can digest cellulose with the help of bacteria.
Although indigestible, yet cellulose is of considerable importance in
human dietetics, because it add bulk to the intestinal contents,
stimulate peristalsis and there by help in the formation and evacuation
of faeces. Filter papers, commonly used in the laboratories, are
almost pure cellulose .
(e) Inulin.
It is a polysaccharide composed of D-fructose units. It
is a white crystalline powder and is readily soluble in hot water. It
dose not give any such characteristic colour with iodine.
 Other polysaccharides containing carbohydrate and non-
carbohydrate units are:
(1) Heteropentosans
(2) Heterohexosans
(3) Mucopolysaccharides are composed of two to six different
monosaccharides units including amino sugar and uronic acid. Many
important biological compounds are included in this group, they are
hyaluronic acid chondroitin sulphate, heparin, blood group
substances, etc. the first three are called acid mucopolysaccharides
due to their acidic character. The mucopolysaccharides in tissues are
usually present in combination with protein and are called
glycoproteins .
 (a) It is the readily available fuel of the body .
(b) It also constitutes the structural material of the organism.
(c) It also acts as important storage of food material of the
organism.
(d) Carbohydrate also plays as a key role in the metabolism
of amino acids and fatty acids.
 Bibliography

Physiology by C.C.Chatargi
Physiology by Gyton and Hall.
Physiology by A.K.Jain.
Physiology by Simbuligam.
Physiology by Genan