IMMUNOLOGY

Detailed explanation-1: -IgG is a monomer with an approximate molecular weight of 146 Kd and a serum concentration of 9.0 mg/mL. IgG is said to be divalent, i.e., it has two identical antigen-binding sites that comprise 2 L chains and 2 H chains joined by disulfide bonds.

Detailed explanation-2: -As a B-cell surface immunoglobulin, IgM exists as a monomer and functions as a receptor for antigens. The surface IgM is structurally different in the Fc region from the secreted form since it must bind through the membrane.

Detailed explanation-3: -The IgG antibody molecule is made up of four polypeptide chains, comprising two identical light chains and two identical heavy chains, and can be thought of as forming a flexible Y-shaped structure.

Detailed explanation-4: -Immunoglobulin domains The Ig monomer is a “Y"-shaped molecule that consists of four polypeptide chains; two identical heavy chains and two identical light chains connected by disulfide bonds. Each chain is composed of structural domains called immunoglobulin domains.