Effect of a heat-stable factor in human placenta on glucosylceramidase, glucosylsphingosine glucosyl hydrolase, and acid beta-glucosidase activities.
Effect of a heat-stable factor in human placenta on glucosylceramidase, glucosylsphingosine glucosyl hydrolase, and acid beta-glucosidase activities.
复制标题
人胎盘中热稳定因子对葡萄糖神经酰胺酶、葡萄糖基鞘氨醇葡萄糖基水解酶和酸性 β-葡萄糖苷酶活性的影响。
DOI：
10.1016/0009-9120(87)90010-5
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发表时间：
1987
影响因子：
2.8
通讯作者：
Suzuki,K
中科院分区：
文献类型：
--
作者：
Vaccaro,AM;Muscillo,M;Tatti,M;Salvioli,R;Gallozzi,E;Suzuki,K
A new protein activator of glucosylceramidase has recently been found in human placenta. In the present work, it has been compared with a previously reported glucosylceramidase activator, the Gaucher factor. The two activators showed different properties. The Gaucher factor stimulated 100% the 4-methylumbelliferyl-β-D-glucopyranoside hydrolysis while the placental factor inhibited it 50%. Furthermore, the placental factor neither decreased the Michaelis constant, Km, nor increased the degree of inactivation by conduritol-β-epoxide as the Gaucher factor does. From these results it has been concluded that the two activators are different substances. The activating effect of the placeental factor is specific for the hydrolysis of glucosylceramide; neither the hydrolysis of glucosylsphingosine nor that of the 4-methylumbelliferyl derivative are enhanced by this protein. Owing to its specificity and high level in a human tissue, the placental factor is likely to have a physiological role in the catabolism of glucosylceramide.
