IMMUNOGLOBULINS

Immunoglobulin are glycoprotein

produced by plasma cells.

IMMUNOGLOBULIN
 BASIC STRUCTURE
1. Each molecule of Ig consists of two pairs of polypeptide
chains of different sizes.
2. Light(L) and heavy(H) chains.
3. Molecular weight of light chain is approximately 25,000.
4. Molecular weight of heavy chain is approximately 50,000.
5. The light and heavy chain are linked by disulphide bonds.
 BASIC STRUCTURE

1. The light chain are similar in all classes of immunoglobulins.

2. They occur in two varieties, kappa and lambda.
3. Light and heavy chains are subdivided into variable and
constant region.
4. Each heavy and light chain contains amino terminal in
variable region, carboxy terminal in constant region.
 CLASSIFICATION

1. IgG –(gamma)
2. IgA-(alpha)
3. IgM-(mu)
4. IgD-(delta)
5. IgE-(epsilon)
 IMMUNOGLOBULIN G
1. Most abundant class in serum.
2. Constitutes 80% total immunoglobulin.
3. Present in blood , plasma and tissue fluids.
4. Contains less carbohydrate than other immunoglobulins.
5. Act against bacteria and viruses by opsonizing.
6. It has a half life of 23 days.
7. Ig G1,Ig G2,Ig G3,Ig G4.
 IMMUNOGLOBULIN A

1. Constitutes 10-15% of total immunoglobulins.

2. Present in milk, saliva, tears, mucous of respiratory
tract, digestive tract.
3. In serum exist as monomer.
4. In external secretions exist as dimer called secretory
immunoglobulin.
5. Half life:6-8 days.
 IMMUNOGLOBULIN M

1. Constitutes 5-10% of total serum proteins.

2. Held together by disulphide bonds and ‘J’ chain.
3. Molecular weight 900,000-10,00,000(millionaire
molecule).
4. Half life:5days.
 IMMUNOGLOBULIN E

1. Structure is similar to Ig G.
2. Has 4 constant region domains.
3. Molecular weight 1,90,000.
4. Heat labile.
5. Normal serum concentration 0.3 ug/ml.
 IMMUNOGLOBULIN D

1. Structure is similar to IgG.

2. Serum concentration 30 micrograms per ml.
3. Constitutes 0.2% of total immunoglobulins.
4. Half life:3days.
5. It is a monomer.
6. It located at B-cell surface , blood and lymph.