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Science 30 January 1976:
Vol. 191. no. 4225, pp. 390 - 392
DOI: 10.1126/science.1246619
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Articles

Science, Vol 191, Issue 4225, 390-392
Copyright © 1976 by American Association for the Advancement of Science

articles

Structure, function, and evolutionary relationships of Fc domains of human immunoglobulins A, G, M, and E

TL Low, YS Liu, and FW Putnam

Human immunoglobulins, A, G, M, and E have strong homology in amino acid sequence (about 30 percent) distributed nonuniformly throughout the Fc region. Immunoglobulins M are A are least alike in the first Fc domain and most alike in the second. Individual domains of heavy chains have evolved with different mutation rates but with conservation of essential structural features. No relation of primary structure to complement binding ability is apparent.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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 »
Complete covalent structure of a human IgA1 immunoglobulin.
Y. Liu, T. Low, A Infante, and F. Putnam (1976)
Science 193, 1017-1020
   Abstract »    PDF »


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