Purification of a phospholipase C from Bacillus cereus.

Phospholipase C activity present in the growth medium of Bacillus ceyeus was purified 2o-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 g kLmoles/min per mg toward purified diacyl glycerophosphoryl ethanolamine and a specific activity of about 15-20 ;tmoles/ min per mg toward diacyl glycerophosphorylmonomethylethanolamine and diacyl glycerophosphoryl choline. Monoacyl glycerophosphate was not hydrolyzed under similar conditions.