Abstract
The reversible binding of the first component of guinea pig complement in its enzymatically active from (Cl̄) ‡ ‡ Abbreviations and symbols for the complement components and for the intermediate products of hte hemolytic sequence follow the recommendations of the WHO Nomenclature Committee (Austen et al., 1970). to antigen-antibody complexes has been measured over a 200-fold range of input Cl̄ concentration. The complexes consisted of dinitrophenylated sheep erythrocytes carrying bound rabbit IgG antibody against the ϵ-N-(2,4-dinitrophenyl)-lysine group. Bound and free Cl̄ were measured separately. The binding of Cl̄ to these complexes shows positive homotropic cooperativity. This cooperative binding is consistent with an allosteric interpretation of antibody function.
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