Studies on sphingomyelinase of Bacillus cereus. I. Purification and properties.
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.
D001409:Bacillus cereus / Q000201:enzymology*; D002413:Cations, Divalent / Q000494:pharmacology; D004910:Erythrocyte Membrane; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D010740:Phospholipases / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification*; D013108:Sphingomyelin Phosphodiesterase / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D002413:Cations, Divalent; D010740:Phospholipases; D010727:Phosphoric Diester Hydrolases; D013108:Sphingomyelin Phosphodiesterase