Dissociation of soluble antigen-antibody complexes by rheumatoid factor IgM.
Intact rheumatoid factor (RF)-active IgM dissociated soluble antigen-antibody complexes formed in the antigen excess zone, whereas trypsin-digested protein had less effect. The dissociation mechanism involved an interaction between the RF IgM and the Fc gamma of antibodies in the complexes. RF-active IgM had no demonstrable effect on antigen-antibody complexes when the antigen or the antibody had been immobilized. This was true irrespective of whether the experiments were performed in the antigen or in the antibody excess zone and despite binding between RF IgM and the immobilized proteins.
D000818:Animals; D000936:Antigen-Antibody Complex / Q000032:analysis* / Q000378:metabolism; D006801:Humans; D007075:Immunoglobulin M / Q000502:physiology*; D011234:Precipitins / Q000032:analysis; D011817:Rabbits; D011961:Receptors, Fc / Q000378:metabolism; D017452:Receptors, IgG; D012217:Rheumatoid Factor / Q000032:analysis / Q000502:physiology*; D012709:Serum Albumin / Q000276:immunology; D014357:Trypsin / Q000494:pharmacology
D000936:Antigen-Antibody Complex; D007075:Immunoglobulin M; D011234:Precipitins; D011961:Receptors, Fc; D017452:Receptors, IgG; D012709:Serum Albumin; D012217:Rheumatoid Factor; D014357:Trypsin