EXPRESSION, PURIFICATION AND CHARACTERIZATION OF A FUNCTIONAL PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C-DELTA-1 PROTEIN IN ESCHERICHIA-COLI

被引：8

作者：

GINGER, RS ^{[1
]}

PARKER, PJ ^{[1
]}

机构：

[1] IMPERIAL CANC RES FUND, POB 123, LINCOLNS INN FIELDS, LONDON WC2A 3PX, ENGLAND

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 210卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb17403.x

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：

Inositol-lipid-specific phospholipase C-delta1 (PtdIns-PLCdelta1) was expressed in Escherichia coli as a fusion protein containing a short 22-amino-acid lac-Z-derived amino terminus. Under appropriate conditions, the phospholipase constituted approximately 0.2% of the detergent-soluble protein and could be purified to near homogeneity in a simple three step protocol. The catalytic properties of the purified enzyme closely resemble those of the eukaryote-derived protein. The suitability of bacterial expression for the investigation of PtdIns-PLCdelta regulation is discussed.

引用

页码：155 / 160

页数：6

共 26 条

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