AN UNUSUAL PHOSPHODIESTERASE ACTIVITY TOWARDS P-NITROPHENYLPHOSPHORYLCHOLINE PRESENT IN RAT-BRAIN MEMBRANES

被引：8

作者：

KANFER, JN

MCCARTNEY, D

机构：

[1] Department of Biochemistry, University of Manitoba, Winnipeg, R3E 0W3, Manitoba

来源：

NEUROCHEMICAL RESEARCH | 1990年 / 15卷 / 10期

关键词：

P-NITROPHENYLPHOSPHORYLCHOLINE; HEAT STABILITY; FATTY ACID ACTIVATABLE;

D O I：

10.1007/BF00965744

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 phosphodiesterase activity present in rat brain membranes has been examined utilizing a p-nitrophenylphosphorylcholine as the substrate. This enzyme activity has a pH optimum of 8.5, is stimulated by a variety of free fatty acids, requires either Zn+2 or Ca+2 and is relatively stable to heating at 75-degrees-C for 7.5 minutes. These properties appear to distinguish this particular activity from those previously reported for alkaline phosphatase, nonspecific phosphodiesterase, phosphodiesterases I and II, lecithinase, and sphingomyelinase.

引用

页码：987 / 992

页数：6

共 25 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] PHOSPHODIESTERASES IN HUMAN TISSUES .1. IDENTIFICATION AND SEPARATION OF ENZYMES ACTIVE ON BIS(P-NITROPHENYL)PHOSPHATE [J].