Mirgorodskaia O A, Tennikova T B, Moskvichev B V
Biokhimiia. 1978 Oct;43(10):1924-8.
The interaction of trypsin with an acid polysaccharide, heparin, at pH 4.2 and 8.0 is studied. Heparin is found to destabilize the enzyme under condition of both autolytic denaturation (pH 8.0) and thermoinactivation (pH 4.2). Data on trypsin inactivation kinetics suggest that the stage of forming molecular complexes with different contents of trypsin and heparin precedes the stage of the enzyme denaturation. Maximal trypsin inactivation rate takes place under equimolar enzyme:heparin ration.
研究了胰蛋白酶与酸性多糖肝素在pH 4.2和8.0条件下的相互作用。发现在自溶变性（pH 8.0）和热失活（pH 4.2）条件下，肝素都会使该酶不稳定。胰蛋白酶失活动力学数据表明，在酶变性阶段之前存在与不同胰蛋白酶和肝素含量形成分子复合物的阶段。在酶与肝素等摩尔比的情况下，胰蛋白酶失活速率达到最大值。
