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. 1975 Dec;72(12):5111–5115. doi: 10.1073/pnas.72.12.5111

Activation of antibody Fc function by antigen-induced conformational changes.

J C Brown, M E Koshland
PMCID: PMC388886  PMID: 1061094

Abstract

IgM antibody directed against the pheny-beta-lactoside hapten was examined for its capacity to fix complement in the presence of the hapten, monohapten-substituted antigen, and multihapten-substituted antigen. Hapten was found to have no effect; monovalent antigen induced an excellent response which could be inhibited by hapten; and multivalent antigen also induced an excellent response which was related to the number of determinants added and not to the formation of antigen-antibody aggregates. The difference between the activities of hapten and monovalent antigen was reflected in their affinities for the IgM antibody. The monovalent antigen had a lower Ka, indicating that energy from binding was used to activate the Fc complement binding sites. These data show that the expression of IgM Fc function depends on a change in Fc conformation produced by the binding of antigen at the distant Fab combining sites.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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