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The Journal of Immunology, 1966, 97: 319-330.
Copyright © 1966 by The American Association of Immunologists, Inc.

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Reactions of Human Anti-{gamma}-Globulin Factors with Digested and Urea-Reduced {gamma}-Chains1

Thomas G. Lawrence, Jr.2 and Ralph C. Williams, Jr.3

From The Arthritis Unit, University Hospitals, Minneapolis, Minnesota

Abstract

Digestion of {gamma}-chains by trypsin, chymotrypsin, and bacterial protease produced a spectrum of changes in antigenic determinants revealed by the fine specificity of human rheumatoid factors as sources of 19S antibody to human IgG. Gm(a) activity was greatly reduced by chymotrypsin and bacterial protease digestion of {gamma}-chains. Trypsin digests of {gamma}-chains retained inhibitory capacity for both Gm(a) and Gm(b1) systems. By contrast, changes produced by reduction in 4 to 8 M urea did not destroy Gm(a) activity, but abolished Gm(b1) activity. These findings were amplified by digestion and urea reduction of {gamma}-chains from Gm(a)+ and Gm(b1) + myeloma proteins.

Footnotes

1 Aided by grants 1 T1 AM 5461 and AM 07372 from United States Public Health Service and from the Minnesota Arthritis Foundation.

2 United States Public Health Service, Arthritis Trainee, Arthritis Unit, University of Minnesota Hospitals, Minneapolis, Minnesota.

3 Associate Professor of Medicine, University of Minnesota Hospitals, Minneapolis, Minnesota.







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