• Proteins: Berzelius first coined the term in 1838 which

means ‘first order’ or prime importance.

• They are complex organic nitrogenous compounds.
• Amino acids are the building blocks of proteins, they
are joined together by means of a peptide bond
resulting in the formation of protein. Proteins are
synthesized on the ribosomes. The proteins are
needed for growth and maintenance of body. The
sources of protein are milk, cheese, pulses, peanuts,
fish, meat etc.
• The twenty amino acids are:
Valine, Leucine & Isoleucine; Alanine, Arginine,
Glutamine, Lysine, Aspartic acid, Glutamic Acid
, Proline, Cysteine, Threonine,
Methionine, Histidine, Phenylalanine, Tyrosine,
Tryptophan, Asparagine, Glycine, Serine.
• Phenylalanine, threonine, tryptophan, leucine,
isoleucine, histidine, lysine, methionine and
valine are the essential amino acids which
cannot be synthesized in our body and must be
taken through our diet, while non-essential
amino acids can be synthesized by our body.
Zwitter ion of amino acid
• This is called a zwitterion. This is the form that amino
acids exist in even in the solid state. If you dissolve
the amino acid in water, a simple solution also contains
this ion. A zwitterion is a compound with no overall
electrical charge, but which contains separate parts which
are positively and negatively charged.
• The structure of an amino acid allows it to act as both
an acid and a base. An amino acid has this ability because
at a certain pH value (different for each amino acid) nearly
all the amino acid molecules exist as zwitterions. One of
the most useful applications of zwitterions is in SDS PAGE
which is one of the most common practical procedures in
molecular biology. It is a form of electrophoresis used to
separate protein molecules by molecular mass
• Proteins can be monomeric i.e., contain one polypeptide
chain ex: lysozyme, myoglobin etc.
• They can be multimeric, containing many polypeptide chains
ex; Hemoglobin has 2 α and 2 β chains; Insulin has one α and
one β chain.
• They can also be classified as :
• i) complete proteins: which have all essential and non-
essential amino acids, ex: beef, animal proteins.
• ii) incomplete proteins: lack some as essential amino acids,
ex: plant proteins.

• A peptide bond is a chemical bond formed between two

molecules when the carboxyl group of one amino acid reacts
with the amino group of the second amino acid, releasing a
molecule of water (H2O).
• All proteins known to exist in living beings are
made of 20 amino acids. Each protein has a
characteristic 3-dimensional shape, called
conformation.
•  
• 1.Primary structure: is the number and sequence
of the amino acids held together by peptide bonds
in a polypeptide chain. This sequence is strictly
controlled by the sequences of bases in DNA. A
change in the sequence creates a different protein,
and the sequence of amino acids in a protein
determines its function and biological activity.
• 2. Secondary structure: interactions between
the amino acids of the primary structure lead to
folding, kinking, or even pleating of the sheets.
Side by side polypeptide chains are cross-
linked by hydrogen bonds.
• The polypeptide chains exhibit three types of
arrangement like α -helical, β -pleated sheet
and random.
• Linus Pauling discovered the alpha helix
structure in proteins and was awarded the
Nobel Prize in 1954.
• In an α helix, the carbonyl (C=O) of one amino
acid is hydrogen bonded to the amino H (N-H)
of an amino acid that is four down the chain.
(E.g., the carbonyl of amino acid 1 would form
a hydrogen bond to the N-H of amino acid 5.)
This pattern of bonding pulls the polypeptide
chain into a helical structure that resembles a
curled ribbon, with each turn of the helix
containing 3.6 amino acids. Ex: Keratin in hair,
nails, feathers are examples of alpha helix.
• In a β pleated sheet, two or more segments of a
polypeptide chain line up next to each other,
forming a sheet-like structure held together by
hydrogen bonds. The hydrogen bonds form between
carbonyl and amino groups of backbone, while the R
groups extend above and below the plane of the
sheet. The strands of a β pleated sheet may
be parallel, pointing in the same direction (meaning
that their N- and C-termini match up),
or antiparallel, pointing in opposite directions
(meaning that the N-terminus of one strand is
positioned next to the C-terminus of the other). Ex:
silk fibroin of silk worms is an example of this.
• Random: The polypeptide chain does not show geometrical
order. The lack of geometry is due folding of the amino acid
side chains rather than the folding of polypeptide chain.
• Tertiary structure: It is the three dimensional conformation of
a polypeptide. highly intricate spheres or globules are formed
by the interaction of ionic, hydrogen, vander Waal’s and
electrostatic interactions, disulphide bonds as well as
hydrophobic interaction. Two shapes of tertiary structure are
globular and fibrous. Ex: myoglobin

• Quartenary structure: Some of the proteins contain two or

more polypeptide chains called subunits. The spatial
arrangement of these subunits is called quaternary structure.
Ex: haemoglobin protein has 2 α and two βchains.
•  
QUATERNARY STRUCURE OF HEMOGLOBIN
Genetic Codon Table
A point mutation where GAA (Glu) is
replaced by GUA (Val)
• Proteins are classified as fibrous and globular based
on shape.
• Fibrous proteins: have no tertiary structure, they
are long parallel polypeptide chains and are
insoluble in water, very tough and carry out
structural functions, found in connective tissue,
tendons, matrix of bones (collagen) in muscles,
spider ‘s webs and silk worm cocoons etc. And as
keratin in the hair nails, feathers and horns
• Globular proteins: have complex tertiary and
quartenary structures. Ex are immunoglobulins
proteins, hormones and some enzymes. These
proteins unlike fibrous proteins are soluble in water.
• On the basis of solubility proteins are classified into:
• A) Simple proteins: on hydrolysis yields only amino acids. Six types of
simple proteins :
• 1. Albumins: soluble in water and dilute salt solutions. Egg albumin,
serum albumin from blood,β-amylase etc
• 2. Globulins: insoluble or sparingly soluble in water. Soluble in dilute
salt solutions. Myosin of muscles and serum globulins are examples.
• 3. Glutelins: Insoluble in neutral solutions but are soluble in weak acid
or basic solutions. Found in cereal grains.
• 4. Prolamines: insoluble in water, but soluble in 70 to 80 percent
ethanol. On hydrolysis these proteins yield proline and ammonia, ex:
zein of maize, gliadin of wheat and hordein of barley.
• 5. Histones: soluble in water, rich in basic amino acids like lysine and
arginine, are found in cell nuclei.
• 6. Protamines: rich in basic amino acids, found in nucleus associated
with nucleic acids
• B) Conjugated proteins: contain a non amino acid component (prosthetic
group). They are six types:

• 1. Nucleoproteins: on hydrolysis yield nucleic acid plus asimple protein,

nucleic acid proteins of ribosomes and chromosomes.

• 2. Glycoproteins: contain carbohydrate as prosthetic group such as mucin

and some proteins of plasma membrane.
• 3. Lipoproteins: are conjugates of lipids. Components of membranes.

• 4. Chromoproteins: chlorophyll proteins and hemoglobins. Prosthetic group

is a pigment.

• 5. Metalloproteins: many enzymes require metal as an activator ex ferritin.

• 6. Phosphoproteins : contain phosphate group linked ex is casein from milk.

• C) Derived proteins: These are derived from
simple or conjugated proteins by chemical or
enzymatic reaction. Examples are peptones,
proteoses, and polypeptides. A proteose is any of
various water-soluble compounds that are
produced during digestion by the hydrolytic
breakdown of proteins short of the amino acid
stage. It forms after breaking down of
polypeptides by gastric pepsin. In addition
to proteoses, peptones are also formed at this
stage.
• Derived Proteins
• Derived from simple or compound proteins by denaturation
or some chemical reaction such as hydrolysis.
• They are subdivided into Primary & Secondary derived
proteins.
• Primary Derived Proteins These are denatured or co-agulated
proteins.
Example : Egg proteins.
Secondary Derived Proteins. These are intermediates formed in
protein hydrolysis.
Examples are :
• Proteoses
• Peptones
• Polypeptides
• Oligopeptides
• Some important proteins and their functions:
• Structural proteins like collagen are insoluble and serve as
supporting material. Collagen forms skin, cartilage, ligaments,
tendons etc, while scales of fish and reptiles and hair, feather,
horns are made of keratin.
• Transport proteins are carrier proteins which move molecules
from one place to another around the body. Hemoglobin is
one of these and is responsible for transporting oxygen
through the blood via red blood cells. Cytochromes are
another that operate in the electron transport chain as
electron carrier proteins.
• Antibodies are specialized proteins involved in defending the
body from antigens (foreign invaders). They can travel through
the bloodstream and are utilized by the immune system to
identify and defend against bacteria, viruses, and other foreign
intruders.
• Enymatic proteins : act as enzymes and function in
regulating biochemical reactions, ex: lipase which
catalyses the hydrolysis of fats to fatty acids and
glycerol.
• Hormonal proteins are messenger proteins which
help to coordinate certain bodily activities.
Examples include insulin, oxytocin, and
somatotropin.
• Insulin regulates glucose metabolism by controlling
the blood-sugar concentration. Oxytocin stimulates
contractions during childbirth. 
• Contractile proteins are responsible for muscle
 contraction and movement. Examples of these
proteins include actin and myosin.
• Denaturation of proteins: In biological systems, a protein has
a unique 3-D structure and a unique biological activity. This is
the native form of protein. If a protein in native form is
subjected to a physical change (change in temperature) or
chemical change (pH change), hydrogen bonds are broken, the
disturbance unfolds the protein globules and uncoils the helix of
the protein molecule. The protein loses its biological activity,
this is called denaturation.
• The secondary and tertiary structure of the protein are destroyed
but the primary structure remains same. The globular proteins
are converted to fibrous proteins hence denaturation leads to
coagulation, ex: coagulation of egg white when egg is boiled.
• Enzymes:
• Enzymes are biological catalysts which accelerate the
rate of biochemical reaction, produced in living cells
only.
• First predicted by Berzelius in 1835, Kuhne in 1878 used
the term enzyme, J.B Sumner isolated the enzyme
urease in jack bean meal, Northrop isolated pepsin,
trypsin and chymotrypsin. Digestion of food, absorption
of appropriate molecules and production of energy all
these reactions need enzymes. Enzymes are very
specific for a particular reaction and they are named
after the compound on which they act.
• Ex : Maltase catalyses hydrolysis of maltose into
glucose. Dehydrogenases remove hydrogen.
•  Enzymes are protein molecules of high molecular weight.
Two general types of structure of enzyme molecules:
• 1) Simple protein molecules : proteins containing only
amino acids.
• 2) Conjugated protein molecules: proteins with attached
non-protein groups. It has two parts: i) apoenzyme:
composed of amino acids only and ii) prosthetic group- a
non protein group. The enzyme molecule consisting the
protein and prosthetic group is Holoenzyme. The
prosthetic group may be an inorganic cofactor or organic
coenzyme. The metals known to be cofactors of enzymes
are copper, iron, manganese, zinc, calcium etc.
• Organic coenzymes are nicotinamide dinucleotide (NAD)
coenzyme A etc.
• Nearly all enzymes are proteins, although a few catalytically
active RNA molecules have been identified.
• Enzyme catalyzed reactions usually take place under relatively
mild conditions (temperatures well below 100 oC, atmospheric
pressure and neutral pH) as compared with the corresponding
chemical reactions.
• Enzymes are biocatalysts that increase the rate of a chemical
reaction without being changed themselves in the process.
• Enzymes are highly specific with respect to the substrates on
which they act and the products that they form.
• Enzyme activity can be regulated, varying in response to the
concentration of substrates or other molecules.
• They function under strict conditions of temperature and pH
in the body.
• Many enzymes require the presence of small, non-protein units or
cofactors to carry out their particular reaction.
• Cofactors may be either one or more inorganic ions, such as
Zn2+ or Fe2+ or a complex organic molecule called a coenzyme. Ex
Fe is required for activation of cytochrome oxidase.
• A metal or coenzyme that is covalently attached to the enzyme is
called a prosthetic group (heme in hemoglobin).
• Some coenzymes, such as NAD+, are bound and released by the
enzyme during its catalytic cycle and in effect function as co-
substrates. Many coenzymes are derived from vitamin precursors.
• A complete catalytically-active enzyme together with its coenzyme
or metal ion is called a holoenzyme.
• The protein part of the enzyme on its own without its cofactor is
termed an apoenzyme.
• Properties of enzymes:
• 1) They are active in very small amounts. The
number of moles of substrate converted per minute
by one mole of enzyme is called turnover number of
the enzyme.
• 2) Enzymes remain unaffected by the reaction they
catalyze.
• 3) An enzyme hastens the completion of reaction,
but it does not affect the equilibrium of the reaction.
• 4) They are very specific in nature.
• 5) Being proteins, they can loose their activity on
heating, i.e., thermolabile.
• Nomenclature and classification of enzymes: e. For example,
dehydrogenases remove hydrogen atoms, proteases hydrolyze
proteins, and isomerases catalyze rearrangements in configuration.
• Systematic nomenclature and classification of enzymes was given by
International Union of Biochemistry in 1995. Main features are:
• 1) All enzymes are divided into six major classes: Viz.,
Oxidoreductases, transferases, hydrolases, lyases, isomerases and
ligases.
• Oxidoreductases catalyse oxido-reduction reactions , oxidize their
substrate by addition of oxygen, removal of hydrogen or electrons.
Ex: cytochrome oxidase
• Transferases : transfer of a functional group such as amino,
phosphate thiol group from one molecule to another. Ex:
Hexokinase
• Hydrolases: Catalyse the the hydrolytic cleavage of C-C, C-O, C-N, P-O
bonds of their substrate by addition of water. Ex: amylase, lactase,
maltase.
• Lyases: Catalyse the removal of groups from their substrate. Ex:
decarboxylases remove CO2 group and hydrases remove water ex: aldolase,
histidine decarboxylase. C-C, C-O, C-N, and other bonds by elimination.

• Isomearses: Substrate is converted into its geometric or structural changes

within the same molecule.ex: triose phosphate isomerase, malate
isomerase.

• Ligases: catalyse the linking together of compounds using ATP as energy

source. Ex: DNA ligase; pyruvate carboxylase catalyses bond between
pyruvate and carbondioxide to form oxaloacetate.
• The name of the enzyme has two parts, the first denotes the name of the
substrate and the second ending in ‘—ase’ indicates the type of the reaction
catalysed.
•  
• .
• Functions of enzymes:
• Enzymes are biocatalysts, which means they speed up
the rate at which reactants interact to form products in
a chemical reaction. To do this, enzymes lower the
activation energy required for bonds to break and new
bonds to form, making the formation of a product
much faster. Without enzymes, these chemical
reactions would proceed at a rate that is hundreds to
thousands of times slower.
• Zymogens are precursors of enzymes. They are the
inactive forms and become active after conversion ( for
ex: cleavage by certain enzymes like trypsin converts
chymotrypsinogen to is active form) . CT breaks
proteins and peptides in pancreas.
• Two theories
• 1) Lock and key hypothesis (by Emil Fischer,1894) and Induced
fit hypothesis( By D. Koshland, 1966) explain the mechanism
of enzyme action.
• The substance on which the enzyme acts is called substrate
and the substance obtained at the end of reaction is called
product. Enzymes are mostly globular proteins and have their
primary, secondary, tertiary or quartenary structures. The
Lock and Key hypothesis states that the enzyme and its
substrate have a complementary shape, substrate binds to the
active site and a complex is formed.
E + S -------- ES ---------- E + P e=enzyme,
S=substrate, P=product.
A particular lock(substrate) can be opened by a Particular key
(enzyme)
• Induced Fit Hypothesis: Koshland proposed it. The active site of the enzyme
does not a exist in a shape that is complementary to the substrate. Enzyme
is induced to assume a complementary shape according to the substrate
configuration, like a kind of ‘glove and hand relationship’.
• Different enzymes show features of both models, with some
complementarity and some conformational change.

• Factors affecting enzyme activity:

• Substrate concentration: If other conditions are constant, an increase in the
substrate concentration increases the rate of the enzyme catalysed reaction.
• Enzyme concentration: If the substrate is in excess, an increase in the
enzyme concentration , increases the rate of the reaction.
• Temperature: Due to their proteinaceous nature enzymes are sensitive to
temperature changes and their activity is confined to a narrow temperature
range. Enzymes show a temperature optimum which is between 30°C and
50°C.
• pH: Most enzymes have an optimum pH range of 4 to 9. Pepsin is active at
acidic pH 2.0 while trypsin is active at pH 8.2.
•The substrate(s) is bound in the active site by multiple weak forces
which result into the enzyme-substrate complex.

•Once bound active residues within the active site of the enzyme act on
the substrate molecule to transform it first into the transition state
complex and then into product, which is released.

•The enzyme is now free to bind another molecule of substrate and

begin its catalytic cycle again
• The active site of an enzyme is the region that binds the substrate and
converts it into product.
• It is usually a relatively small part of the whole enzyme molecule and is a
three-dimensional entity formed by amino acid residues that can lie far
apart in the linear polypeptide chain.
• The active site is often a cleft or crevice on the surface of the enzyme that
forms a predominantly nonpolar environment which enhances the binding
of the substrate.
• The substrate(s) is bound in the active site by multiple weak forces
(electrostatic interactions, hydrogen bonds, van der Waals bonds,
hydrophobic interactions; and in some cases by reversible covalent bonds.
• The enzymes can bind to substances other than substrate, which results in
inactivation of the enzyme. These are called inhibitors and they compete
with the substrate for binding to the same site on the enzyme, this can be
reversed by increasing the substrate concentration. This is called competitive
inhibition.
• In non-competitive inhibition, the inhibitor binds to different site and cannot
be reversed by increasing substrate concentration.
• Isoenzymes are different forms of an enzyme which catalyze the
same reaction, but which exhibit different physical or kinetic
properties, such as isoelectric point, pH optimum, substrate affinity
or effect of inhibitors.
• Different isoenzyme forms of a given enzyme are usually derived
from different genes and often occur in different tissues of the
body, for example LDH-2 is present in white cells, while LDH-5 in
liver and skeletal muscle.
• An example of an enzyme which has different isoenzyme forms is
lactate dehydrogenase (LDH) which catalyzes the reversible
conversion of pyruvate into lactate in the presence of the coenzyme
NADH and is used as a marker of cell damage or cell death.
• LDH is a tetramer of two different types of subunits, called H and M,
which have small differences in amino acid sequence. The two
subunits can combine randomly with each other, forming five
isoenzymes that have the compositions H4, H3M, H2M2, HM3 and M4.
The five isoenzymes can be resolved electrophoretically.
• Significance of Enzymes
• In the absence of an enzyme, biochemical reactions hardly proceed at all,
whereas in its presence the rate can be increased up to 107-fold. Thus, they
are crucial for normal metabolism of living systems. The enzymes in your
body help to perform very important tasks. These include building muscle,
destroying toxins, and breaking down food particles during digestion

• Besides in the body, extracted and purified enzymes have many

applications.
• Medical applications of enzymes include:
• Enzymes are markers in various disease states such as jaundice, cancer,
pacreatitis.
• To treat enzyme related disorders.
• To assist in metabolism
• To assist in drug delivery.
• To diagnose & detect diseases.
• In manufacture of medicines.
• Industrial applications of enzymes include: Enzymes are widely
used by the food industry for processing raw materials for the
production of numerous and common products such as dairy,
bakery products, meat products, fruit products, beer and wine.

• Amylase, lactases, cellulases are enzymes used to break

complex sugars into simple sugars.
• Pectinase like enzymes which act on hard pectin is used in fruit
juice manufacture.
• Lipase enzymes act on lipids to break them in fatty acids and
glycerol. Lipases are used to remove stains of grease, oils,
butter.
• Enzymes are used in detergents and washing soaps.
• Protease enzymes are used to remove stains of protein nature
like blood, sweat etc.
• Vitamins may be defined as a group of biomolecules,  most of which cannot be
produced by the body and must be supplied in small amounts in diet to perform the
specific biological function for the life, growth and health of humans beings and
animal organisms.
• Example: Vitamin A, Vitamin K, Vitamin B etc.
• Vitamins neither supply energy nor help in building tissue of the cell but their
deficiency
• in the body can cause serious diseases.
• Plants can synthesize all Vitamins but animals can synthesize very few vitamins. Some
vitamins are present in the nature also, like vitamin D which is either supplied by
food or may be produced in the skin by the irradiation of ergosterol with ultraviolet
light.
• Human body can also synthesize some vitamin A from carotenes, some components
of vitamin B complex and vitamin K are synthesized by microorganisms present in the
intestinal tract.
• The main sources of vitamins are our food which consists of milk, butter, green
vegetables, meat, eggs etc.
•  Vitamins are also synthesized in the laboratory and are available in the form of
tablets, capsules, which can be taken orally or as with injection as prescribed in the
case of vitamin deficiency.
• Classification of Vitamins
• Vitamins are complex organic molecules. They are broadly classified into the following two
categories: Water soluble and Fat Soluble
• Water Soluble Vitamins: These vitamins are water soluble. These vitamins must be supplied
regularly in diet because they are regularly excreted in urine and cannot be stored in our
body.
• Vitamin B1: Its chemical name is Thiamine,
• Source: It is found in pulses, nut, whole cereals, rice polishing, yeast, egg yolk, milk, green
vegetables and in fruits.
• Deficiency Diseases: Their deficiencies cause Beriberi disease, in which legs get paralysed and
cause loss of appetite.
• Vitamin B2: Its chemical name is Riboflavin or Lactoflavin. Characteristics: It is sensitive to
light but stable to heat. It is essential for growth and health of animals.
• Sources: It is found in milk, yeast, green vegetables, meat, liver, kidney etc.
• Deficiency Diseases: Its deficiency retards growth, and cause general inflammation of tongue,
dermatitis and cheilosis.
• Vitamin B6: Its chemical name is Pyridoxine. In fact
it is a mixture of pyridoxine, pyridoxal and
pyridoxamine. Source: It is found in rice bran, yeast,
molasses, meat, fish etc.
• Deficiency Disease: It causes specific dermatitis in
rats, pellagra and anaemia in human beings, affects
central nervous system, causes general weakness,
convulsions, weakness, nervousness, insomnia and
irritability.
• Vitamin B12: Its chemical name is
as cyanocobalamin. It contains cobalt. Source: It is
found in milk, eggs and liver of ox, sheep, pig etc.
• Deficiency Disease: It causes pernicious anaemia,
inflammation of tongue and mouth.
• Vitamin C: Its chemical name is Ascorbic acid.

• Characteristics: It is destroyed by cooking and prolonged exposure to air. To

avoid the loss, vegetables riches in vitamin C must be cooked in closed pan
and pressure cooker. Vitamin C increases resistance of the body towards
diseases, maintains healthy skin and helps cuts and abrasion to heal
properly. Vitamin C, also known as ascorbic acid, is necessary for the growth,
development and repair of all body tissues. It's involved in many body
functions, including formation of collagen, absorption of iron, the immune
system, wound healing, and the maintenance of cartilage, bones, and teeth.
• For adults, the recommended daily amount for vitamin C is 65 to 90
milligrams (mg) a day, and the upper limit is 2,000 mg a day.
• Source: It is found in citrus fruits, lemons, leafy vegetables, chillies, sprouted
pulses and germinated grains.
• Deficiency Disease: It causes scurvy, pyorrhoea.
• Fat Soluble Vitamins: These vitamins are the oily substance and not readily soluble
in water, however they are soluble in fat. Excess intake of these vitamins is harmful
for health and may cause hypervitaminoses.

• Vitamin A: Its chemical name is Retinol. Carotenoids are precursors of vitamin A.

Vitamin A has multiple functions: it is important for growth and development, for
the maintenance of the immune system, and for good vision.
• Sources: It is present in milk, butter, eggs, fish liver oil, rice polishing, green
vegetables etc.
• Deficiency Disease: Its deficiency causes Xerophthalamia, night blindness and
xerosis.

• Vitamin D: Its chemical name is ergocalciferol and commonly called  Sunshine

Vitamin. It controls calcium and phosphorus metabolism.
• Vitamin D is essential for several reasons, including maintaining healthy bones and
teeth. It may also protect against a range of diseases and conditions, such as
type 1 diabetes.
• Sources: It is present in fish liver oils, butter, milk, eggs, liver and meat. Daily dose
of vitamin D in human body is about 0.025 mg.
• Deficiency Diseases: Its deficiency causes rickets in children and oestromalacia in
adults.
• Vitamin E: It is a mixture of four vitamins called α, β, ϒ, ᵟ- tocopherols.
Characteristics: It is stable to heat and oxidation.
• Sources:  Its sources are vegetable oils (like wheat germ oil, cotton seed oil,
soybean oil, peanut oil etc.), eggs, milk etc. Its daily dose to human body is about
15mg.
• Vitamin E has the following functions: It is an antioxidant. This means it protects
body tissue from damage caused by substances called free radicals. Free radicals
can harm cells, tissues, and organs.
• Deficiency Disease: Its deficiency causes sterility, increased fragility of RBCs and
weakness.

• Vitamin K: Its chemical name is phylloquinone and commonly called

as Antihaemorrhagic Vitamin. And it is a mixture of two vitamins called K1 and K2.
play a role in blood clotting, bone metabolism, and regulating blood calcium levels.
The body needs vitamin K to produce prothrombin, a protein and clotting factor
that is important in blood clotting and bone metabolism. Daily dose is 90
microgram per day for females and 120 micrograms per day for males.
• Sources: Vitamin K1- alfalfa, leafy vegetables and spinach. Vitamin K2- occurs
mainly in bacteria.
• Deficiency Disease: Its deficiency cause haemorrhage, it lengthens the time of
blood clotting