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Science 22 March 1968:
Vol. 159. no. 3821, pp. 1355 - 1357
DOI: 10.1126/science.159.3821.1355
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Articles

Two-Chain Immunoglobulin A Molecules: Abnormal or Normal Intermediates in Synthesis

Rose Lieberman 1, J. Frederic Mushinski 2, and Michael Potter 2

1 National Institute of Allergy and Infectious Diseases, Bethesda, Maryland
2 National Cancer Institute

Immunoglobulin A (ggrA) myeloma proteins secreted by plasma-cell tumors of mice are of two types, a common four-chain molecule and a rare two-chain (3.9S) molecule. The close similarity between two-chain ggrA molecules and four-chain ggrA molecules and their polymers is demonstrated in tryptic peptide maps of isolated polypeptide chains and by precipitin reactions with rabbit antiserums to ggrA immzunoglobulins. However, a difference between these two types is distinguishable with homologous antiserums. Homologous antiserums to two-chain ggrA immunoglobulins are specific and do not cross-react with four-chain ggrA immutnoglobulins.


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 »
Immunoglobulin M Heavy Chain Disease: Intracellular Origin of the Mu Chain Fragment.
J. Buxbaum, E. C. Franklin, and M. D. Scharff (1970)
Science 169, 770-773
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)