title: Action of D-penicillamine on immunocomplexes containing rheumatoid factor.
abstract: The affinity between purified rheumatoid factors (RF) and native or heat aggregated human IgG has been studied in vitro by polarization fluorescence in the presence and in the absence of D-penicillamine. The value of the dissociation constant was the same using native and heat aggregated IgG suggesting that binding to the aggregated protein is not dependent on the exposure of a new determinant lacking in the native molecule. The results obtained in the presence of D-penicillamine suggest that the concentration of the drug necessary to get a pronounced effect on the apparent dissociation constant of the immunocomplex between IgG and RF is not reached in vivo, in clinical situations.
mesh_terms: D000936:Antigen-Antibody Complex / Q000378:metabolism*; D000937:Antigen-Antibody Reactions / Q000187:drug effects; D001172:Arthritis, Rheumatoid / Q000188:drug therapy* / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D066298:In Vitro Techniques; D010396:Penicillamine / Q000494:pharmacology*; D012217:Rheumatoid Factor / Q000378:metabolism*
chemical_list: D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D012217:Rheumatoid Factor; D010396:Penicillamine