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The Reaction of Rheumatoid Factor and Complement with -Globulin Coated Latex

From the Department of Medicine, University of Colorado, Denver, Colorado

Abstract

A modification of the rheumatoid latex fixation test which involves photometric measurements of the supernatant permitted plotting of agglutination curves and was used to characterize the "reactant" globulin. Both unaggregated electrophoretically obtained human -globulin and commercially prepared Cohn Fraction II were found to be suitable reactants. Heating Cohn Fraction II reduced the spontaneous precipitation of the coated latex. It was suggested that the heating process, in addition to slightly denaturing Cohn Fraction II, partially deaggregated it. Data were obtained which showed a relatively low and variable protein-binding capacity for latex, from 2.6 to 12.4 µg of -globulin nitrogen/mg of latex. The variation in protein adsorption was attributed to heterogeneity of the -globulin, since protein adsorbed to latex was firmly bound and did not exchange measurably with another protein added later. Despite the evidence that only a small fraction of the -globulin added in the test procedure was adsorbed to latex, excess -globulin did not inhibit the agglutination test. It was therefore postulated that a close apposition of -globulin molecules on the latex surface increased the strength of rheumatoid factor attachment, and that complement and rheumatoid factor attached to the same sites on the aggregated -globulin. Additional evidence given in favor of this concept included the fixation of complement by -globulin coated latex and the presence in fresh serum of a heat-labile inhibitor. On the other hand, data were also presented suggesting slight differences between the specificity of complement and rheumatoid factor for sites on aggregated -globulin.

Footnotes

¹ This work was done during the senior author's tenure of fellowship from the National Foundation and was supported by Grant E-3047 from the National Institute of Allergy and Infectious Diseases, National Institutes of Health, United States Public Health Service, Bethesda, Maryland.