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.
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 12 Jan 1976|