Psychrophilic trypsin-type protease from Serratia proteamaculans

被引：10

作者：

Mikhailova, A. G.

Likhareva, V. V.

Khairullin, R. F.

Lubenets, N. L.

Rumsh, L. D.

Demidyuk, I. V.

Kostrov, S. V.

机构：

[1] Russian Acad Sci, Shemyakin & Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

[2] Russian Acad Sci, Inst Mol Genet, Moscow 123182, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2006年 / 71卷 / 05期

基金：

俄罗斯基础研究基金会;

关键词：

psychrophilic enzymes; trypsin; Serratia proteamaculans; affinity chromatography; substrate-inhibitor analysis;

D O I：

10.1134/S0006297906050166

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A preparative method for purification of a novel protease from the psychrotolerant Gram-negative microorganism Serratia proteamaculans (PSP) was developed using affinity chromatography on BPTI-Sepharose. It yielded electrophoretically homogeneous PSP preparation of 60 kD. The PSP properties (temperature and pH stability, high catalytic efficiency) indicate that this enzyme can be defined as a psychrophilic protease. Inhibitory analysis together with substrate specificity indicates that the studied PSP exhibits properties of serine trypsin-like and Zn-dependent protease.

引用

页码：563 / 570

页数：8

共 26 条

[1]

[Anonymous], 1970, Methods in Enzymology, DOI DOI 10.1016/0076-6879(70)19005-7

[2]

ASGEIRSSON B, 1989, EUR J BIOCHEM, V180, P85

[3] CATALYTIC AND BINDING-SITES OF PORCINE ENTEROPEPTIDASE [J].