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Structure Of Immunoglobulin

Introduction

Constitute the gamma globulin portion of blood proteins
Are soluble proteins secreted by activated B cells and plasma cells in response to an antigen
Are capable of binding specifically with that antigen

Function

Bind its antigen
Direct it towards other components of the Immune System so that it can be destroyed.

Immunoglobulin molecule:

Represents hetero-tetrameric quarternary structure between 4 polypeptide (2 heavy + 2 light) chains
Y-shaped
VL = Variable domain of light chain.
CL = Constant domain of light chain.
VH = Variable domain of a heavy chain
CH = Constant domain of a heavy chain
S-S = Disulphide bond.

Constant region/Carboxy terminus

Constant unit
Fc fragment of Ig

Determines the biological properties of Ig:

Complement fixation
Placental transfer
Skin fixation
Catabolic rate

Amino terminus/Variable unit/FAB/ANTIGEN BINDING SITE

Antigen binding site
Composed of both L and H chains

Highly variable zones

Hypervariable regions or Hotspot
Involved in the formation of antigen-binding sites.
Sites on the hypervariable regions which make actual contact with the epitope
Are called complementarity determining regions or CDR’s

Heavy chain

Have high molecular weight i.e 50,000-77,000d
Composed of 450 amino acid
Class specific antigenic determinants of an immunoglobulin is associated with H-chain
H chain consist of 1 variable (VH) and three domains in constant region (CH1, CH₂,CH₃)
CH2 region in IgG & IgM binds C1q in the classical complement sequence
CH3 domain mediates monocyte adherence

Immunoglobulin class	Heavy chain
IgG	γ (gamma)
IgA	α (alpha)
IgM	μ(mu)
IgD	δ(delta)
IgE	ε (epsilon)

Light chain

Molecular weight 25000
Composed of 212 amino acid
Light chain further divides into either kappa or lambda.
Immunoglobulin may contain either kappa or lambda but not both
L chain consists of 1 variable V_L and 1 constant domain C₁

Disulfide bond

Light and heavy chain are joined to each other by disulfide bond

Hinge region

The area of the H chain in the C region between the first and second C region domains (CHI and CH2).
Papain acts in the hinge region
Splits each Ig molecule into 3 parts: 1 Fc and 2 Fab
Pepsin digests Fc portion, resulting in a 5S portion – 2 Fab fragments held together: F(ab)2

Exam Important

STRUCTURE OF ANTIBODIES:

Immunoglobulin molecule:

Represents hetero-tetrameric quarternary structure between 4 polypeptide (2 heavy + 2 light) chains

CONSTANT REGION/CARBOXY TERMINUS

Fc fragment of Ig
Determines the biological properties of Ig
- Complement fixation
- Placental transfer
- Skin fixation
- Catabolic rate

Amino terminus/Variable unit/FAB/ANTIGEN BINDING SITE

Antigen binding site

Heavy chain

have high molecular weight i.e 50,000-77,000d
Composed of 450 amino acid.

Class specific antigenic determinants of an immunoglobulin is associated with H-chain

H chain consist of 1 variable (VH) and three domains in constant region (CH1, CH₂,
CH₃
Highly variable zones
- 3 in L and 4 in H chain
- Involved in the formation of antigen-binding sites.
- Sites on the hypervariable regions which make actual contact with the epitope
- Are called complementarity determining regions or CDR’s

CH2 region in IgG & IgM binds C1q in the classical complement sequence

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Structure Of Immunoglobulin