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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 VA. 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
Annual Review of Immunology – Annual Reviews
Published: Apr 1, 1985
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