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Science 10 September 1976:
Vol. 193. no. 4257, pp. 1017 - 1020
DOI: 10.1126/science.821146
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Articles

Science, Vol 193, Issue 4257, 1017-1020
Copyright © 1976 by American Association for the Advancement of Science

articles

Complete covalent structure of a human IgA1 immunoglobulin

YS Liu, TL Low, A Infante, and FW Putnam

The complete covalent structure has been determined for a human myeloma IgA1 immunoglobulin. This protein has unique features in the amino acid sequence and disulfide bridge structure of the variable (V) and constant (C) regions of both the alpha heavy and the lambda light chains, and in the number and loci of oligosaccharides. Whereas C region domains of heavy chains have evolved independently over eons, recent isotypic variations have occured in lambda light chains and possibly in alpha heavy chains.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Cysteine Residues Required for the Attachment of the Light Chain in Human IgA2.
K. R. Chintalacharuvu, L. J. Yu, N. Bhola, K. Kobayashi, C. Z. Fernandez, and S. L. Morrison (2002)
J. Immunol. 169, 5072-5077
   Abstract »    Full Text »    PDF »
Plasma Cell Leukemia with Excretion of Half-Molecules of Immunoglobulin A ({alpha}1 {lambda}1).
G. M. BERNIER, J. H. BERMAN, and M. W. FANGER (1977)
Ann Intern Med 86, 572-575
   Abstract »    PDF »


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