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The Biologic Activities of Denatured Human IgG and its Heavy Chains

Department of Internal Medicine and Physical Therapy, Faculty of Medicine, University of Tokyo, Tokyo, Japan

Abstract

tH (polymerized H-chain) of human IgG did not show skin-fixing activity in the guinea pig as judged by RPCA. The structures of pU-IgG (polymerized urea-treated IgG) and tH required for reactivity with rheumatoid factors are not related to the IgG site needed for skin fixation. tH does not increase vascular permeability. The results suggest that the skin-fixing site of IgG is dependent upon its three-dimensional structure and is easily lost by many modifications. On the other hand, the modified structure of IgG and H-chain exhibits reactivity with rheumatoid factors, but only non-alkylated, reduced and aggregated IgG increases vascular permeability. These results strongly suggest that newly-created conformational structures are essential for development of the ability to increase vascular permeability in the guinea pig skin and reactivity with rheumatoid factors, but that these structures are not identical.