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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Jun;74(6):2531–2535. doi: 10.1073/pnas.74.6.2531

Conversion of incomplete antibodies to direct agglutinins by mild reduction: evidence for segmental flexibility within the Fc fragment of immunoglobulin G.

D G Romans, C A Tilley, M C Crookston, R E Falk, K J Dorrington
PMCID: PMC432207  PMID: 267947

Abstract

Reduction of interchain disulfide bonds converted some IgG incomplete antibodies to direct hemagglutinins. This conversion occurred whether antibody was free in solution or bound to the red-cell surface. Reduced antibody permitted to reoxidize in air no longer behaved as a direct agglutinin; reversion to an incomplete antibody did not occur when reoxidation was prevented by S-alkylation. These results suggest that mild reduction of the antibody imparts sufficient freedom to permit bridging between cells and are interpreted as evidence that the interheavy-chain disulfide bonds restrict segmental flexibility within the Fc fragment of IgG.

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Selected References

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