PURIFICATION OF A PHOSPHOLIPASE C FROM BACILLUS CEREUS

被引:47
作者
KLEIMAN, JH
LANDS, WEM
机构
[1] Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich
关键词
D O I
10.1016/0005-2760(69)90044-7
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
Phospholipase C activity present in the growth medium of Bacillus cereus was purified 20-fold by chromatography on polyethyleneimine-cellulose columns, or by treatment with protamine sulfate and subsequent chromatography on DEAE-cellulose columns. Purified enzyme preparations retained the ability to hydrolyze ethanolamine phosphoglycerides in the absence of choline phosphoglycerides. A typical preparation had a specific activity of about 9 μmoles/min per mg toward purified diacyl glycerophosphoryl ethanolamine and a specific activity of about 15-20 μmoles/ min per mg toward diacyl glycerophosphorylmonomethylethanolamine and diacyl glycerophosphoryl choline. Monoacyl glycerophosphate was not hydrolyzed under similar conditions. © 1969.
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页码:477 / &
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