丁酸梭菌M 55中两种蛋白酶的纯化及部分特性分析

Purification and partial characterization of two proteinases from Clostridium butyricum M 55.

作者信息

Ciborowski P, Hryniewicz W, Jeljaszewicz J

机构信息

Department of Bacteriology, National Institute of Hygiene, Warsaw, Poland.

出版信息

Zentralbl Bakteriol Mikrobiol Hyg A. 1988 Apr;268(2):180-92. doi: 10.1016/s0176-6724(88)80002-6.

DOI:10.1016/s0176-6724(88)80002-6

PMID:3293333

Abstract

Clostridium butyricum M55 proteinases were purified by application of a multistep procedure involving ethanol precipitation, DEAE cellulose chromatography and molecular sieving. The purified enzymes obtained were called proteinase I and proteinase II. They appeared to be homogeneous when examined by molecular sieving and polyacrylamide gel electrophoresis. The highly purified proteinases were studied for their physico-chemical properties. The influences of pH, temperature, ionic strength and amino acids composition were investigated. The effects of metal ions and of protein-structure-modifying agents support views suggesting the character of these enzymes.

摘要

通过采用包括乙醇沉淀、DEAE纤维素色谱法和分子筛在内的多步程序，对丁酸梭菌M55蛋白酶进行了纯化。得到的纯化酶分别称为蛋白酶I和蛋白酶II。通过分子筛和聚丙烯酰胺凝胶电泳检测时，它们似乎是均一的。对高度纯化的蛋白酶的物理化学性质进行了研究。研究了pH、温度、离子强度和氨基酸组成的影响。金属离子和蛋白质结构修饰剂的作用支持了表明这些酶特性的观点。