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From the Department of Experimental Pathology, Scripps Clinic and Research Foundation, and the Salk Institute for Biological Studies, La Jolla, California 92037
Abstract
Mouse IgA myeloma proteins have been studied for the structure of their polypeptide chains and papain fragments. Heavy and light chains, Fab and Fc fragments were shown to have molecular weights closely corresponding to their IgG equivalents and the mass ratio of Fab and Fc fragments indicate the presence of two Fab and one Fc fragments per IgA monomer. The results, taken together with the available hapten-binding data, suggest that a single light-heavy chain pair constitute a hapten-binding site in IgA. In addition, structural studies performed on normal mouse IgA indicate the presence in their structure of dimerized light chain as had been previously reported for IgA myeloma proteins.
Footnotes
1 This is publication 387 from the Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California. This investigation was supported by United States Public Health Service Grants from the National Institutes of Health, A1-07007, A1-05875 and Training Grant 5213 to Dr. Melvin H. Cohn, Atomic Energy Commission Contract AT(04-3)-410 and American Heart Association Grant 67-795.
2 Established Investigator of the American Heart Association. Current address: Division of Allergy and Clinical Immunology, National Jewish Hospital and Respiratory Center, Denver, Colorado 80206.
3 All reprint inquiries should be addressed to Dr. H. M. Grey, Division of Allergy and Clinical Immunology, National Jewish Hospital and Respiratory Center, 3800 East Colfax Avenue, Denver, Colorado 80206.
4 Recipient of a United States Public Health Service Training Grant GM-00702.
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