A phospholipase specific for sphingomyelin from Clostridium perfringens.
作者： I Pastan , V Macchia , R Katzen
DOI: 10.1016/S0021-9258(19)34202-4
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摘要: Abstract An enzyme that hydrolyzes sphingomyelin to ceramide and phosphorylcholine has been purified from the growth medium of Clostridium perfringens. The activity is stimulated about 2-fold by magnesium chloride diethyl ether. completely inhibited 10-3 m ethylenediaminetetraacetic acid or calcium chloride. Lysolecithin dipalmitoyl lecithin are hydrolyzed at 10% rate sphingomyelin. No hydrolysis phosphatidylserine, phosphatidyl-ethanolamine, phosphatidylinositol detected. does not catalyze exchange phosphorylcholine-14C into
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