Ikezawa H, Mori M, Ohyabu T, Taguchi R
Biochim Biophys Acta. 1978 Feb 27;528(2):247-56.
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.
通过硫酸铵沉淀以及在CM-葡聚糖凝胶、二乙氨基乙基纤维素和葡聚糖凝胶G-75上进行层析，从蜡状芽孢杆菌的培养液中纯化出一种鞘磷脂酶，纯化倍数为980倍，回收率为25.6%。纯化后的制剂不含脂肪酶、蛋白酶和其他磷脂酶。该酶特异性地将鞘磷脂水解为神经酰胺和磷酸胆碱。溶血磷脂酰胆碱也会受到该酶的作用。该酶（分子量=24000）在pH 6至7时活性最高。还报道了该酶的其他特性，包括溶血活性以及激活/抑制研究。
