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From the
1 From the Department of Biochemistry, the Hebrew University-Hadassah Medical School, Jerusalem, Israel
An enzyme was extracted from rat brain particles and was purified 18-fold. It hydrolyzed sphingomyelin (1-O-phosphorylcholine-2-N-acylsphingosine) to ceramide (N-acylsphingosine) and phosphorylcholine, but did not catalyze the hydrolysis of lecithin. The reaction was not reversible and had a pH optimum of 5.0 and a Km of 1.3 x 10-4 M. The enzyme hydrolyzed sphingomyelins with D-erythro-sphingosine or dihydrosphingosine 3 to 5 times faster than those with D-threo or L-erythro configuration. It was inhibited by ceramide, sphingosine, and fatty acid, but not by phosphorylcholine. Sphingomyelin could be hydrolyzed to sphingosine, fatty acid, and phosphorylcholine by the combined action of this enzyme and of "ceramidase."
Submitted on September 27, 1965
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