Abstract
Through a study of the myeloma proteins of man, and induced antibodies and myeloma proteins in other species, a comprehensive understanding of the relationship of the structure of immunoglobulin molecules and their function is emerging. The domain hypothesis, originally proposed by Edelman in the late 1960’s is now on firm experimental ground (1). The variable domain, consisting of VH and VL is the area of the antigen binding site (2, 3). This is a pocket or groove in the three-dimensional structure which is lined by the hypervariable regions (4-6). A large body of experimental data indicates that the idiotypic determinants generally derive from the structures of the hypervariable regions and thus, by inference, antibody combining site. An Fc region can be produced from each immunoglobulin class and certain defined biological functions can be ascribed to it. Furthermore, the Fc region of each class has a distinctly different biological activity. In the IgG and IgM class, each of the separate Fc domains has been isolated and separately tested for biological activity. Complement fixing regions, and neutrophil, macrophage, and mast cell binding areas of the immunoglobulin molecule are known in general terms (7).
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Siegelman, M., Capra, J.D. (1979). Immunoglobulin Structure and Function: Idiotypy and the Oligoclonal Response. In: Karcher, D., Lowenthal, A., Strosberg, A.D. (eds) Humoral Immunity in Neurological Diseases. NATO ASI Series, vol 24. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1003-7_40
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DOI: https://doi.org/10.1007/978-1-4684-1003-7_40
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