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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.