STUDIES ON SPHINGOMYELINASE OF BACILLUS-CEREUS .1. PURIFICATION AND PROPERTIES
- 1 January 1978
- journal article
- research article
- Vol. 528 (2) , 247-256
Abstract
A sphingomyelinase [EC 3.1.4.12.] was purified 980-fold with recovery of 25.6% from the culture broth of B. cereus, by (NH4)2SO4 precipitation and chromatography on CM-Sephadex, DEAE-cellulose and Sephadex G-75. The purified preparation was free of lipase, protease and other phospholipases. The enzyme specifically hydrolyzed sphingomyelin to ceramide and phosphorylcholine. Lysophosphatidylcholine was also attacked by the enzyme. The enzyme was maximally active at pH 6-7. Other properties of the enzyme, including hemolytic activity and activation/inhibition studies, are reported.This publication has 8 references indexed in Scilit:
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