BIOL 53700 Study Guide - Midterm Guide: Immunoglobulin Therapy, Intron, Syk

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The igg antibody molecule is made up of four polypeptide chains, comprising two identical light chains and two identical heavy chains that form a flexible y-shaped structure. Each of the four chains has a variable region at its amino terminus, which contributes to the antigen-binding site, and a constant region. Two antigen-binding sites allow antibody molecules to cross-link antigens and to bind them much more stably and with higher avidity. The trunk of the y, also called the fc fragment, is composed of the carboxy-terminal domains of the heavy chains, and it is these domains that determine the antibody"s isotype. Joining the arms of the y to the trunk are the flexible hinge regions. The fc fragment and hinge regions differ in antibodies of different isotypes. Different isotypes have different properties and therefore differ in their interactions with effector molecules and cell types. However, the overall organization is similar in all isotypes.

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