Abstract
Summary Digestion of γ-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 γ-chains. Trypsin digests of γ-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 γ-chains from Gm(a)+ and Gm(b1) + myeloma proteins.
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