Ultracentrifugal studies of the reactions of rheumatoid factor with native human gamma-G-globulin.

Analytical ultracentrifugation has been employed in a study of the effect of pH on the dissociation of the 22S complexes formed between isolated rheumatoid factor and native human γG-globulin (prepared from autologous and isologous rheumatoid sera and from normal sera). The results indicate that rheumatoid factor has equal avidity for each of the γG-globulins tested irrespective of their source. The possibility that native human γG-globulin is a `haptenic' form of aggregated γG-globulin is discussed.