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γ-GLOBULINS OR IMMUNOGLOBULINS
These are proteins which functions as
antibodies or are chemically related to
antibodies.
The immunoglobulin molecule is a Y shaped
molecule having two identical heavy chains
(H) and two identical light chains (L) linked
together by disulfide bridges.
Immunoglobulin Function
The primary function of immunoglobulin
molecules are to bind "foreign" proteins,
carbohydrates, nucleic acids and glycolipids so
that they can be cleared from the organism by
cells specialized to perform such processes.
Immunoglobulins typically bind antigens and
are found in extracellular fluids, a variety of
body secretions, and attached to the outer
surface of cell membranes
 Light Chains (L)
Each L chain that has two recognizable
regions:
 C-terminal region (about half) that is
nearly constant in most immunoglobulins.
Slight variations in this region produce 2
isotypes called kappa (к) and lambda (λ).
 N-terminal region that varies
considerably from one immunoglobulin to
the next.
Heavy Chains (H)
The size of H chains varies with immunoglobulin
class. Heavy chains determine the immunoglobulin
class e.g. in Ig G (γ), Ig A (α) Ig M (μ) ,Ig D (δ) and Ig E
(ε).
H chains also have variable and constant regions in
their amino acid sequences.
The constant region is the C-terminal three-fourths
of the polypeptide. Slight variations of this region
also produce H chain isotypes.
The variable region is the N-terminal one-fourth of
the polypeptide.
 Immunoglobulins
There are two antigen combining sites per
unit known as F(ab)2 piece, lying at the
ends of arms of Y.
Both L and H chains are necessary for full
antibody activity.
Each immunoglobulin has two binding sites
Immunoglobulin Molecule
Enzyme Papain splits the immunoglobulin molecule into three
pieces of equal size.
Two of these pieces are identical and are able to bind antigen,
the third piece is different and is not capable of antigen
binding but can bind proteins found in complement.
 Cont….
 The H chains are associated with a variable
amount of carbohydrate, Ig M has the
highest content.
 Some immunoglobulin molecules may
contain more than one unit usually bound
together by J chains e.g. Ig M.
 Characteristics of the immunoglobulins .
Class Heavy Mean plasma Molecular Function
Chain Concentration (g/L) Weight (kDa)

IgG γ 14.0 146 The major antibody of secondary

immune responses
IgA α 3.5 160 The major antibody in seromucous
secretions, e.g. saliva, bronchial
mucus

IgM μ 1.5 970 Confined to the vascular spaces the

major antibody of the primary immune
response

IgD & 0.03 184 Present on the surface of B

lymphocytes, involved in antigen
recognition

IgE ε trace 188 Present on surface of mast cells and

Basophils, probable role in immunity to
helminths and associated with
immediate hypersensitivity reactions
Immunoglobulins (1- Ig G )
γ2 к2 or γ2 λ2 has a molecular weight of
150,000 and average normal concentration
in serum 10 g/L, it forms about 80% of total
immunoglobulin.
Ig G level rises slightly later in response to
bacterial toxins. Because of their relatively
low molecular weight they can diffuse freely
into interstitial fluid and act in tissues
against infection.
 2. Ig A
It is α2 к2 or α2 λ2 having molecular weight of
385,000 having concentration of 2.5 g/L forming 13% of
total immunoglobulins.
It is synthesized submucosally and is present in
intestinal and respiratory secretions, sweat, tears and
colostrum.
It also exists in polymeric form mainly dimer but
some trimer in which monomers are linked by a J
chain.
It is affected more than other immunoglobulin in
diseases of gastrointestinal and respiratory tracts.
 3. Ig M
- μ2к2 or μ2λ2 having molecular weight of
900,000 has normal plasma concentration of 1.0
g/L forming about 6% of total immunoglobulins.
Ig M is synthesized first in response to
particular antigens such as blood borne
infections.
Because of their large size they are almost
confined to intravascular compartment making
first line of defense against blood borne
infections.
The fetus can synthesize Ig M and high levels at
birth indicate that there have been some
intrauterine infections.
 4. Ig D
- δ2к2 or δ2λ2 having molecular weight of
180,000 has plasma concentration of less than
150 mg/L forming about 1% of total
immunoglobulins.
Ig D was found to bind to basophils and mast
cells and activate these cells to produce
antimicrobial factors to participate in
respiratory immune defense in humans.
It also stimulates basophils to release B cell
homeostatic factors.
 5. Ig E
ε2к2 or ε2 λ2 has a molecular weight of
200,000 having plasma concentration of
less than 60 μg/L forming about .002% of
total immunoglobulins.
Ig E is synthesized by plasma cells beneath
the mucosa of GI and respiratory tract and
lymphoid tissue of nasopharynx.
It is present in nasal and bronchial
secretions.
 Cont….
Circulating Ig E is rapidly bound to cell
surfaces particularly to those of mast cells
and circulating basophils so plasma levels are
very low.
Combination of antigen with this cell bound
antibody results is cells releasing mediators
and account for immediate hypersensitivity
reaction.
 Cont…..
Desensitization therapy in allergic disorders
aims at stimulating production of circulating Ig
G against the offending antigen to prevent it
reaching cell bound IgE and/or suppression of
IgE synthesis.
Raised concentrations are found in several
diseases with an allergic component such as
some cases of eczema, asthma and parasitic
infections.
FUNCTIONS
Various immunoglobulins are synthesized by
cells of lymphoid series.
B-lymphocytes when challenged by antigen
undergo a change into plasma cells which are
active synthesizers and secretors of
immunoglobulins, B lymphocytes themselves
may produce a little immunoglobulin which is
present on their surface.
A particular plasma cell and its progeny
referred to as clone produces only one class of
immunoglobulin with a unique structure in
variable part of light and heavy chains.
 Cont….
Other test of BJ proteins is Bradshaw’s
test. To few ml of urine in test tube
concentrated HCL is added along side of
test tube, a white ring is formed at
junction of two, albumin in excess may
also form such ring but in diluted urine
ring is only formed by Bence Jones
proteins.