Cultures of Clostridium perfringens produce a factor which hydrolyzes phospholipids. In this paper we report the separation and the purification from the growth medium of Clostridium perfringens of two phospholipase activities: a specific sphingomyelinase, and a specific lecithinase. Both the phospholipase activities have been purified 300-fold by fractionation of the growth medium with ammonium sulfate, filtration on Sephadex G-100 and chromatography on DEAE cellulose. The sphingomyelinase activity is completely inhibited by 10(-3) M calcium chloride, hydrolyzed lysolecithin and dipalmitoyllecithin at about 10% of the rate of sphingomyelin. No hydrolysis of phosphatidylserine, phosphatidylethanolamine or phosphatidylinositol is detected. From the same growth medium a theta-toxin activity was also purified.
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