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  • Title: Studies on sphingomyelinase of Bacillus cereus. I. Purification and properties.
    Author: Ikezawa H, Mori M, Ohyabu T, Taguchi R.
    Journal: Biochim Biophys Acta; 1978 Feb 27; 528(2):247-56. PubMed ID: 23854.
    Abstract:
    A sphingomyelinase was purified 980-fold with recovery of 25.6% from the culture broth of Bacillus 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 (Mr = 24 000) was maximally active at pH 6-7. Other properties of the enzyme, including hemolytic activity and activation/inhibition studies, are reported.
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