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- W7381591 abstract "Immunoglobulin light (L) chains and L chain genes may seem the poor man’s version of the heavy (H) chains: the specificity of some antibody combining sites may appear to reside largely in the H chain portion (Zhu et al. 1984), most of the secreted camel antibodies even function without L chains (Hamers-Casterman et al. 1993), and terminal deoxynucleotidyl transferase may (in humans) or may not (in mouse) add N regions to L chain (Victor and Capra 1994; Milstein et al. 1992) — it is as if L chain junctional diversity were secondary in importance to that of the H chain. Nonetheless, it is in the L chain system that complementarity-determining regions (CDR) were initially recognized (Wu and Kabat 1970), that immunoglobulin (Ig) gene rearrangement was demonstrated (Hozumi and Tonegawa 1976); it is also where somatic hypermutation in antibody sequences was first deduced (Weigert et al. 1970) and where the phenomenon of gene conversion in vertebrates was discovered (Reynaud et al. 1987). L chain genes may thus be viewed as genetically stripped-down versions of H chain genes that can better serve to elucidate genetic and evolutionary trends in antibody structure and diversity." @default.
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- W7381591 date "2000-01-01" @default.
- W7381591 modified "2023-10-06" @default.
- W7381591 title "Evolution and Somatic Diversification of Immunoglobulin Light Chains" @default.
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- W7381591 doi "https://doi.org/10.1007/978-3-642-59674-2_13" @default.
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