Zoology · Ch 8 — Immunology
Antibodies
Antibodies
Antibodies are immunoglobulin (Ig) proteins synthesised in response to antigen exposure, and each one binds specifically to the antigen that provoked its production. Whenever a pathogen enters the body, B lymphocytes differentiate into plasma cells, which secrete an army of these antibody proteins to neutralise it. Based on their physiological and biochemical properties, antibodies fall into five major classes: IgG (gamma), IgM (mu), IgA (alpha), IgD (delta) and IgE (epsilon).
Structurally, an antibody monomer is a Y-shaped molecule built from four polypeptide chains: two identical light (L) chains (about 25,000 Da, roughly 214 amino acids each) and two identical, larger heavy (H) chains (about 50,000 Da, roughly 450 amino acids each), all held together by disulphide (S–S) bonds — one light chain pairs with each heavy chain, and the two heavy chains join each other, giving the whole molecule the formula H₂L₂. The heavy chains carry a flexible hinge region roughly at their midpoint, which is what lets the two 'arms' of the Y splay apart to grip antigen at different angles. …
What this figure shows. This figure diagrams the Y-shaped structure of an immunoglobulin (antibody) monomer, labelling the two identical heavy chains and two identical light chains linked by disulphide bonds, the variable region at the tips of each arm that forms the antigen-binding site, the constant region forming the stem of the molecule, and the overall H2L2 four-chain architecture that lets each antibody monomer present two iden …