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. 1971 Nov;68(11):2730-3.
doi: 10.1073/pnas.68.11.2730.

Homotropic cooperative binding of the first component of guinea pig complement to rabbit IgG-erythrocyte complexes: a possible allosteric effect

J J Thompson, L G Hoffmann

Homotropic cooperative binding of the first component of guinea pig complement to rabbit IgG-erythrocyte complexes: a possible allosteric effect

J J Thompson et al. Proc Natl Acad Sci U S A. 1971 Nov.

Abstract

Binding of the activated first component of guinea pig complement to immune complexes formed between dinitrophenylated erythrocytes and rabbit IgG antibody to 2,4-dinitrophenylhapten has been studied quantitatively. Cooperative binding was observed; it in volves no interactions between the domains on the erythrocyte surface that bind the activated first component of complement, or between the activated complement molecules in solution. By curve-fitting methods, we find that the data are consistent with an allosteric model, which assumes 10 binding sites per domain, a low allosteric equilibrium constant, and virtually exclusive binding to one of the isomers.

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