Interaction of human α1‐antichymotrypsin with chymotrypsin

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Abstract
Human .alpha.1-antichymotrypsin reacts with bovine chymotrypsin to form an equimolar complex and this reaction is accompanied by the formation of a free, modified form of the inhibitor. Time-course studies, performed on mixtures containing an excess of native inhibitor and kept at 0.degree. C or at 25.degree. C, show that the equimolar complex dissociates spontaneously; this dissociation results in the release of inactive modified .alpha.1-antichymotrypsin and of some active enzyme, which is able to recycle with active inhibitor in excess. When all the native inhibitor is used up, the released active enzyme degrades the remaining intact complex into intermediate forms. At the endpoint of the reaction only inactive modified inhibitor and some active chymotrypsin remain. Immunochemical data indicate that, in the complex, a steric hindrance of the antigenic determinants of the inhibitor prevents the formation of the precipitate with specific antiserum. Inactive modified inhibitor, which has dissociated from the complex, retains antigenic determinants of the native .alpha.1-antichymotrypsin.

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