ANFS332 Lecture Notes - Lecture 23: Immunoglobulin Heavy Chain, Fragment Crystallizable Region, Fragment Antigen-Binding
27 Nov 2016
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Document Summary
Antibody structure, antibody diversity, antibody function, class switching. Immunoglobulins are composed of four polypeptide chains: two light chains (lambda or kappa), and two heavy chains (alpha, delta, gamma, epsilon or mu): the type of heavy chain determines the immunoglobulin isotype (iga, igd, igg, Ige, igm): each chain has constant and variable regions. Variable regions are contained within the amino (nh2) terminal end of the polypeptide chain. When comparing one antibody to another, these amino acid sequences are quite distinct. Constant regions are rather uniform: hypervariable regions are found within the variable regions of both the heavy and light chains. Immunoglobulin function: antibodies function in a variety of ways designed to eliminate the antigen that elicited their production. Some of these functions are independent of the particular class (isotype) of immunoglobulin go against all antigens. For example, an antibody might bind to a toxin and prevent that toxin from entering host cells where its biological effects would be activated.
