A phospholipase specific for sphingomyelin from Clostridium perfringens.

An enzyme that hydrolyzes sphingomyelin to ceramide and phosphorylcholine has been purified from the growth medium of Clostridium perfringens. The activity of the enzyme is stimulated about Z-fold by magnesium chloride and by diethyl ether. The activity of the enzyme is completely inhibited by 10M3 M ethylenediaminetetraacetic acid or 10-3 M calcium chloride. Lysolecithin and dipahnitoyl lecithin are hydrolyzed at about 10% of the rate of sphingomyelin. No hydrolysis of phosphatidylserine, phosphatidylethanolamine, or phosphatidylinositol is detected. The enzyme does not catalyze the exchange of phosphorylcholineX! into sphingomyelin.