Dissociation of Soluble Antigen--Antibody Complexes by Rheumatoid Factor IgM.

Autor:	Alkner, U.
Předmět:	IMMUNOGLOBULINS RHEUMATOID factor IMMUNOGLOBULIN M IMMUNE complexes IMMOBILIZED proteins IMMUNOLOGY
Zdroj:	Scandinavian Journal of Immunology; Aug1983, Vol. 18 Issue 2, p131-136, 6p
Abstrakt:	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 Fey 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. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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