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Dissociation of Soluble Antigen—Antibody Complexes by Rheumatoid Factor IgM
Author(s) -
ALKNER U.
Publication year - 1983
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1983.tb00849.x
Subject(s) - rheumatoid factor , antibody , antigen , chemistry , immunology , dissociation (chemistry) , antigen antibody complex , medicine , organic chemistry
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 Feγ 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.