SHEEP BRAIN PSEUDOCHOLINESTERASE - INHIBITION-KINETICS OF THE PARTIALLY PURIFIED ENZYME BY SOME SUBSTRATE-ANALOGS

被引：4
|
作者：
COKUGRAS, AN
TEZCAN, EF
机构：
[1] Department of Biochemistry, Faculty of Medicine, Hacettepe University, Ankara
来源：
CHEMICO-BIOLOGICAL INTERACTIONS | 1993年 / 87卷 / 1-3期
关键词：
SHEEP BRAIN; PSEUDOCHOLINESTERASE INHIBITION; CHOLINE; SUCCINYLCHOLINE; BENZOYLCHOLINE;
D O I：
10.1016/0009-2797(93)90052-Z
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：
Pseudocholinesterase (ChE) (acylcholineacylhydrolase, EC 3.1.1.8) has been partially purified (about 270-fold) from sheep brain. The procedure included ammonium sulfate fractionation (20 - 80%), DEAE-Trisacryl M chromatography and procainamide-Sepharose 4B affinity chromatography. The molecular weight of purified ChE was found to be 290 000 by gel filtration. Kinetic properties of the enzyme have been studied using the substrate analogues choline, succinylcholine and benzoylcholine. It was shown that the inhibition was partially competitive.
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页码：259 / 264
页数：6
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