Magnesium-dependent sphingomyelinase

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92 Scopus citations


An enzyme which requires divalent metals and hydrolyses sphingomyelin to ceramide and phosphorylcholine is present in rat and human brain and practically absent from other organs. The greatest activity is associated with the microsomal fraction. It had an optimal pH at about 7.4, required magnesium or manganese ions and was completely inhibited by EDTA. Triton X-100 was required for optimal activity and this detergent could also be used to partly solubilize the enzyme from rat brain microsomes. Lecithin was hydrolyzed at only 2% of the corresponding rate of hydrolysis of sphingomyelin.

Original languageEnglish
Pages (from-to)235-241
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 12 Jan 1976
Externally publishedYes


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