A NOVEL METHOD FOR THE PURIFICATION OF PORCINE PHOSPHOLIPASE-A2 EXPRESSED IN ESCHERICHIA-COLI

被引：16

作者：

BHAT, KM

SUMNER, IG

PERRY, BN

COLLINS, ME

PICKERSGILL, RW

GOODENOUGH, PW

机构：

[1] AFRC Institute of Food Research, Reading Laboratory, Shinfield, Reading

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 01期

关键词：

D O I：

10.1016/0006-291X(91)90934-Y

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：

Porcine phospholipaseA2 expressed in E.coli as a fusion protein was isolated, renatured and specifically cleaved by trypsin as described in (1). Active phospholipaseA2, was purified to homogeneity on a column of PBE-94 over a pH region 7.4-4.5. Using this method, several phospholipase A2 mutant enzymes have now been purified in a single step and all behaved identically during chromatofocusing. The method will therefore be extremely useful not only for those interested in understanding the structure-function relationships of phospholipaseA2 but also for preparing the enzyme in large quantities for industrial and pharmaceutical purposes. © 1991.

引用

页码：371 / 377

页数：7

共 14 条

[1] EXPRESSION OF PORCINE PANCREATIC PHOSPHOLIPASE-A2 - GENERATION OF ACTIVE ENZYME BY SEQUENCE-SPECIFIC CLEAVAGE OF A HYBRID PROTEIN FROM ESCHERICHIA-COLI [J].