Interaction of C3 and C3b with immunoglobulin G

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36 Citations (Scopus)

Abstract

Human C3b as well as native C3 were found to bind to solid phase human and rabbit IgG. Haemolytically active C3 had significantly higher binding capacity to IgG than the C3b fragment. Inhibition experiments proved that C3 and C3b have common binding sites on the Fab and Fc part of the IgG molecule but the character of these binding sites was different. As a functional consequence of C3-IgG interaction, C3 binding was found to inhibit the specific precipitation of an IgG antibody preparation.

Original languageEnglish
Pages (from-to)805-810
Number of pages6
JournalMolecular Immunology
Volume20
Issue number8
DOIs
Publication statusPublished - Aug 1983

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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