[溶组织梭菌胶原酶的分离及特性]

[Isolation and properties of 3 Clostridium histolyticum collagenases].

作者信息

Solov'eva N I, Balaevskaia T O, Makeeva O S, Orekhovich V N

出版信息

Vopr Med Khim. 1980 Sep-Oct;26(5):674-7.

Abstract

The collagenases (I, II and III) have been obtained in a highly purified state from fresh cultural medium of Clostridium histolyticum. The collagenases were similar in their properties to clostridiopeptidase A. The three enzymes differed in their molecular weights, isoelectric points and in some chemical properties. Collagenase II exhibited the most potent hydrolytic activity. Its collagenolytic activity was two-fold higher and the peptidase activity was twenty-fold higher as compared with that of collagenase I. All the three enzymes were inactive towards azocasein and were inhibited by EDTA and cysteine.

摘要

胶原酶（I、II和III）已从溶组织梭菌的新鲜培养基中以高度纯化的状态获得。这些胶原酶在性质上与梭菌肽酶A相似。这三种酶在分子量、等电点和一些化学性质上有所不同。胶原酶II表现出最强的水解活性。与胶原酶I相比，其胶原olytic活性高两倍，肽酶活性高二十倍。这三种酶对偶氮酪蛋白均无活性，并受到EDTA和半胱氨酸的抑制。