Interaction of Rheumatoid Factors with Aggregated Subunits of Human γ-Globulin

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Abstract
Summary: Studies on the reactivity of human γ-globulin for the human rheumatoid factors suggest that the specificity of this reaction derives in part from the aggregated state of the γ-globulin and its component H chains. Native γ-globulin exhibits little, if any, reactivity in hemagglutination or gel diffusion experiments. Aggregated L chain preparations are likewise inactive. In contrast, heat-aggregated γ-globulin and turbid H polypeptide chains, as well as heat-aggregated F and S fragments, react with human rheumatoid factors. The inference has been drawn that the antigenic activity of human γ-globulin, or its subunits, for the rheumatoid factors is intimately associated with a change in the secondary or tertiary structure of these molecules which occurs on aggregation.

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