Question

Explain the structure of immunoglobulin with a suitable diagram.

Answer 1

An antibody molecule is a Y-shaped structure that comprises four polypeptide chains, two identical light chains (L) of molecular weight 25,000 Da (approximately 214 amino acids), and two identical heavy chains (H) of molecular weight 50,000 Da (approximately 450 amino acids). The polypeptide chains are linked together by disulfide (S-S) bonds. One light chain is attached to each heavy chain and two heavy chains are attached to each other to form a Y-shaped structure. Hence, an antibody is represented by H₂ L₂ The heavy chains have a flexible hinge region at their approximate middles Antigen binding

Structure of immunoglobulin

Each chain (L and H) has two terminals They are C – terminal (Carboxyl) and amino or N-terminal. Each chain (L and H) has two regions. They have a variable (V) region at one end and a much larger constant (C) region at the other end. Antibodies responding to different antigens have very different (V) regions but their (C) regions are the same in all antibodies. In each arm of the monomer antibody, the (V) regions of the heavy and light chains combine to form an antigen-binding

site shaped to ‘fit’ a specific antigenic determinant. Consequently, each antibody monomer has two such antigen-binding regions. The (C) regions that form the stem of the antibody monomer determine the antibody class and serve common functions in all antibodies.