作者: Abraham Rimon , Yeheskel Shamash , Benyamin Shapiro
DOI: 10.1016/S0021-9258(18)99676-6
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摘要: Purified α1-proteolytic inhibitor from human plasma was shown to inhibit trypsin, chymotrypsin, plasmin, and thrombin. This is probably identical with the previously known as serum trypsin inhibitor, α1-antitrypsin, or antiplasmin. The enzymes were affected by via two different mechanisms. Trypsin chymotrypsin reacted instantaneously in stoichiometric manner, enzyme substrate had no effect on reaction. inhibition of plasmin thrombin time-dependent nonstoichiometric nature, it retarded presence substrate. Even so, kinetic studies failed show a competition reaction between single site molecule. It therefore suggested that mechanism might be an enzymatic inactivation proteolytic concerned. irreversible sense activity could recovered after acid dissociation enzyme-inhibitor complex. differential titration inhibitory towards all four due molecular entity; this conclusion also high purity preparation. On basis its combination estimated have weight 47,000 comprise about 2% proteins.