从嗜冷假单胞菌中分离出一种细胞外中性蛋白酶。

Isolation of an extracellular neutral proteinase from Pseudomonas fragi.

作者信息

Porzio M A, Pearson A M

出版信息

Biochim Biophys Acta. 1975 Mar 28;384(1):235-41. doi: 10.1016/0005-2744(75)90112-6.

Abstract

A single proteolytic enzyme (EC 3.4.4.-) was isolated from culture supernatants of Pseudomonas fragi with 20% yielded and 60-fold purification by means of stepwise DEAE-Sephadex batch adsorption, ammonium sulfate precipitation, gel filtration and DEAE-cellulose chromatography. The enzyme was Zn-2+ activated and Ca-2+ stabilized, had optimum activity at pH 6.5--8.0 and 40 degrees C. The molecular weight range was 40 000--50 000 as determined by dodecylsulfate gel electrophoresis, gel filtration and Zn assay. This proteinase has properties similar to other extracellular bacterial neutral proteinases.

摘要

从草莓假单胞菌的培养上清液中分离出一种单一的蛋白水解酶（EC 3.4.4.-），通过逐步DEAE-葡聚糖凝胶批量吸附、硫酸铵沉淀、凝胶过滤和DEAE-纤维素色谱法，产率为20%，纯化了60倍。该酶由Zn-2+激活，Ca-2+稳定，在pH 6.5-8.0和40℃时具有最佳活性。通过十二烷基硫酸钠凝胶电泳、凝胶过滤和锌含量测定，其分子量范围为40000-50000。这种蛋白酶具有与其他细胞外细菌中性蛋白酶相似的特性。