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NANAJI DESHMUKH VETERINARY SCIENCE
UNIVERCITY
JABALPURE
COLLEGE OF FISHERY SCIENCE
TOPIC- Antibody types and Function
Introduction
All antibodies are proteins known
as immunoglobulins. An antibody is
defined as “an immunoglobulin
capable of specific combination
with the antigen that caused its
production in a susceptible animal.”
Antibodies are produced by plasma
cells which are differentiated by B
cells, in response to the foreign
proteins, called antigens.
The part of the antigen to
which an antibody binds is
called the epitope. The epitope
is a short amino acid sequence
that the antibody is able to
recognize. Antibodies contain
four polypeptide chains and
are arranged in Y-shape.
Antibody molecule contain 4
polypeptide chains, among them
two are identical heavy chains and
two identical light chains. These
chains are held together by
disulphide bonds, Each part of the
molecule has different functions:
The fab fragment: Fab is for
"fragment antigen binding" this
Fab part of the antibody that binds
to antigens. Variable amino acid
sequences can be seen in this
fragment.
There are five different isotypes of
antibody depending on their
difference in heavy chain. These
includes:
IgG, IgM, IgA, IgD and IgE.
IgG
This is the principle
antibody found in blood
and body fluids. Nearly
75% of the antibody
circulating in the blood
is IgG. IgG is a
monomeric
immunoglobulin, built of
two heavy chains and
two light chains.
IgA
IgA represents about
15% to 20% of
immunoglobulins in
the blood. IgA is
involved in mucosal
immunity and prevent
the colonization of
bacteria in the
digestive and
respiratory tracts
IgM
The IgM isotype is
expressed on the surface
of B cells and it is also
secreted by plasma cells.
IgM present in the form
of polymers where
multiple
immunoglobulins are
covalently linked
together with disulfide
bonds, normally as a
pentamer or occasionally
as a hexamer.
IgD
The function of IgD is
not well known but it
makes up about 1% of
proteins in the plasma
membranes of immature
B-lymphocytes. It is also
in serum in very small
level. It is monomeric in
nature. IgD's function is
currently unknown but it
may function as a
regulatory antigen
receptor.
IgE
IgE is a monomeric
immunoglobulin which is
heat labile and plays an
important role in defending
against parasitic worms. IgE
is mainly responsible for
allergies and this is through
their ability to trigger the
release of chemicals from the
granulocytes when the
antibody reacts with specific
antigen. The IgE antibodies
do not activate complement.
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Antibody types and function

  • 1. NANAJI DESHMUKH VETERINARY SCIENCE UNIVERCITY JABALPURE COLLEGE OF FISHERY SCIENCE TOPIC- Antibody types and Function
  • 2. Introduction All antibodies are proteins known as immunoglobulins. An antibody is defined as “an immunoglobulin capable of specific combination with the antigen that caused its production in a susceptible animal.” Antibodies are produced by plasma cells which are differentiated by B cells, in response to the foreign proteins, called antigens.
  • 3. The part of the antigen to which an antibody binds is called the epitope. The epitope is a short amino acid sequence that the antibody is able to recognize. Antibodies contain four polypeptide chains and are arranged in Y-shape.
  • 4. Antibody molecule contain 4 polypeptide chains, among them two are identical heavy chains and two identical light chains. These chains are held together by disulphide bonds, Each part of the molecule has different functions: The fab fragment: Fab is for "fragment antigen binding" this Fab part of the antibody that binds to antigens. Variable amino acid sequences can be seen in this fragment. There are five different isotypes of antibody depending on their difference in heavy chain. These includes: IgG, IgM, IgA, IgD and IgE.
  • 5. IgG This is the principle antibody found in blood and body fluids. Nearly 75% of the antibody circulating in the blood is IgG. IgG is a monomeric immunoglobulin, built of two heavy chains and two light chains.
  • 6. IgA IgA represents about 15% to 20% of immunoglobulins in the blood. IgA is involved in mucosal immunity and prevent the colonization of bacteria in the digestive and respiratory tracts
  • 7. IgM The IgM isotype is expressed on the surface of B cells and it is also secreted by plasma cells. IgM present in the form of polymers where multiple immunoglobulins are covalently linked together with disulfide bonds, normally as a pentamer or occasionally as a hexamer.
  • 8. IgD The function of IgD is not well known but it makes up about 1% of proteins in the plasma membranes of immature B-lymphocytes. It is also in serum in very small level. It is monomeric in nature. IgD's function is currently unknown but it may function as a regulatory antigen receptor.
  • 9. IgE IgE is a monomeric immunoglobulin which is heat labile and plays an important role in defending against parasitic worms. IgE is mainly responsible for allergies and this is through their ability to trigger the release of chemicals from the granulocytes when the antibody reacts with specific antigen. The IgE antibodies do not activate complement.