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• W2046368374 startingPage "591" @default.
• W2046368374 abstract "In their structural variation immunoglobulins simulate within one species the phylogenetic diversity of other proteins among many species. The homologous elements of immunoglobulin structure comprise two classes of light and five classes of heavy chains, one pair of light and one of heavy being joined covalently into a symmetrical non-hybrid tetrapolypeptide. Each chain is divided into a variable or V region and a constant or C region, and each region is believed to be encoded by a separate gene. The V region is further differentiated into subgroups and idiotypes, and the C region into classes, subclasses and allotypes. Sequence analysis of the classes, subclasses, and subgroups indicates that all diverged early in evolution from a common ancestral gene coding for about 110 residues. Most allotypes reflect point mutations in Man and the higher primates, but it is unknown if the numerous varied idiotypes reflect evolutionary gene expansion or somatic hypermutation or recombination. During evolution the acquisition of an almost infinite variety of specific antibody functions by immunoglobulins has been dependent on gene expansion through duplication and mutation leading to molecular variation of the V region and amplification of the number of C regions. Differentiation of biological function has been facilitated by non-specific interactions of homologous regions and by polymerization." @default.
• W2046368374 created "2016-06-24" @default.
• W2046368374 creator A5073957277 @default.
• W2046368374 date "1972-11-01" @default.
• W2046368374 modified "2023-09-23" @default.
• W2046368374 title "Molecular evolution of human immunoglobulins" @default.
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• W2046368374 doi "https://doi.org/10.1016/0047-2484(72)90007-3" @default.
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