Roy A B
Biochim Biophys Acta. 1979 May 10;568(1):103-10. doi: 10.1016/0005-2744(79)90277-8.
Further studies have been made of the cerebroside sulphatase activity of the sulphatase A (aryl-sulphate sulphohydrolase, EC 3.1.6.1) of ox liver. It is concluded that a cerebroside sulphate-modified form of the enzyme is not produced and that the kinetics of the reaction can be explained by the utilisation of the substrate and accumulation of (SO4)2-. The hypothesis is advanced that this difference between the cerebroside sulphatase and arylsulphatase activities arises from non-polar binding of the cerebroside to the enzyme. Possible reasons for the differences between these results and those of other (Stinshoff, K. and Jatzkewitz, H. (1975) Biochim. Biophys. Acta 377, 126-138) are considered.
对牛肝硫酸酯酶A(芳基硫酸酯硫酸水解酶,EC 3.1.6.1)的脑苷脂硫酸酯酶活性进行了进一步研究。得出的结论是,未产生该酶的脑苷脂硫酸盐修饰形式,并且反应动力学可以通过底物的利用和(SO4)2-的积累来解释。提出了这样的假说,即脑苷脂硫酸酯酶和芳基硫酸酯酶活性之间的这种差异源于脑苷脂与该酶的非极性结合。考虑了这些结果与其他研究(Stinshoff, K.和Jatzkewitz, H.(1975年)《生物化学与生物物理学报》377, 126 - 138)结果之间差异的可能原因。