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• W2140472254 abstract "In inbred mice, immunoglobulins (Igs) with K light (L) chains outnumber those with A. L chains by about 20: 1 ( 1-3). A similar or even greater disproportion is found in mouse myeloma proteins (4). Therefore, amino acid sequence analyses of Ig L chains were initially carried out on K chains. Many VK sequences, but only a single CK sequence, were revealed, in accord with later evidence for many VK1 but only a single CK gene segment (5, 6). Amino acid sequences of A. chains made by myeloma tumors suggested a similar arrangement, except that these sequences could be accounted for by only a single V A. gene, as well as a single CA. gene (7). The extremely limited sequence variability of the A. chains [see (7)] suggested, moreover, that they were not significant contributors to the enormous structural and functional diversity that characterizes murine Igs as a whole. While this viewpoint has not been altered by the subsequent finding of additional A. chain isotypes2 (8-10), the overall theme of this review is that the very simplicity of the inbred mouse A. light-chain system offers special opportunities to learn about some fundamental properties of Igs, namely, structure-function relationships, Ig diversity, and regulation ofIg gene expression. This system may also turn out to contribute to our understanding of the T-cell antigen receptor, since recent findings point to significant structural homologies between gene segments for A. chains and for some receptor subunits ( 1 1 1, 1 12)." @default.
• W2140472254 created "2016-06-24" @default.
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• W2140472254 date "1985-04-01" @default.
• W2140472254 modified "2023-10-12" @default.
• W2140472254 title "Lambda Chains and Genes in Inbred Mice" @default.
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• W2140472254 doi "https://doi.org/10.1146/annurev.iy.03.040185.002005" @default.
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