Phospholipase C catalyzed formation of sphinogomyelin--14C from lecithin and N-(-14C)-oleoyl-sphingosine.
Commercial preparations of Clostreidium perfringens were incubated with phosphatidyl choline and N-1-(-14C) oleoylsphingosine.  A radioactive product was formed which cochromatogramed with spingomyelin standard in three different solvent systems.  Several other phospholipases and phosphatases were unable to catalyze this reaction.  Neither choline, phosphoryl choline, cytidine diphosphate choline nor p-nitrophenyl phosphoryl choline were acitve donors.  Sphingomyelin was only slightly active as a phosphoryl choline donor.
D001409:Bacillus cereus / Q000201:enzymology; D002250:Carbon Radioisotopes; D002855:Chromatography, Thin Layer; D003016:Clostridium perfringens / Q000201:enzymology*; D004530:Egg Yolk; D005260:Female; D009829:Oleic Acids / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology; D013045:Species Specificity; D013109:Sphingomyelins / Q000096:biosynthesis*; D013110:Sphingosine / Q000378:metabolism*
D002250:Carbon Radioisotopes; D009829:Oleic Acids; D010713:Phosphatidylcholines; D013109:Sphingomyelins; D010740:Phospholipases; D013110:Sphingosine