Kanfer J N, Mumford R A, Raghavan S S
Can J Biochem. 1977 Feb;55(2):140-5. doi: 10.1139/o77-022.
Some of the properties of a partially purified particle bound and soluble beta-glucosidase (EC 3.2.1.21) from pig kidney were compared. The soluble beta-glucosidase (1) hydrolyzed 4-methylumbelliferyl-beta-D-glucoside (4-MU-beta-D-glucoside) 17 alpha-estradiol 3beta-glucoside. 17 alpha-estradiol 17beta-glucoside, and salicin, but not glucosylceramide, (2) possessed a broad pH optimum (5.5-7.0), (3) had an isoelectric point of 4.9, and (4) was inhibited by Triton X-100. Several compounds were found to be competitive inhibitors of its hydrolytic activity, gluconolactam and estrone beta-glucoside being the most effective. In contrast, a particulate beta-glucodidase purified from the same tissue (1) had an acidic pH optimum (5.0), (2) was stimulated by sodium taurocholate and 'Gaucher's factor' for the hydrolysis of both 4-MU-beta-glucosidase and glucosylceramide, and (3) was capable of catalyzing a transglucosylation reaction employing 4-MU-beta-D-glucoside or glucosylceramide as the glucosyl donor, and [14C]ceramide as acceptor.
对从猪肾中提取的部分纯化的结合型和可溶性β-葡萄糖苷酶（EC 3.2.1.21）的一些特性进行了比较。可溶性β-葡萄糖苷酶（1）可水解4-甲基伞形酮基-β-D-葡萄糖苷（4-MU-β-D-葡萄糖苷）、17α-雌二醇3β-葡萄糖苷、17α-雌二醇17β-葡萄糖苷和水杨苷，但不能水解葡萄糖神经酰胺；（2）具有较宽的最适pH值（5.5 - 7.0）；（3）等电点为4.9；（4）被 Triton X - 100抑制。发现几种化合物是其水解活性的竞争性抑制剂，其中葡糖醛酸内酯和雌酮β-葡萄糖苷最为有效。相比之下，从同一组织中纯化的颗粒状β-葡萄糖苷酶（1）的最适pH值呈酸性（5.0）；（2）在牛磺胆酸钠和“高雪氏因子”存在时，对4-MU-β-葡萄糖苷酶和葡萄糖神经酰胺的水解有促进作用；（3）能够催化以4-MU-β-D-葡萄糖苷或葡萄糖神经酰胺为葡萄糖基供体、[14C]神经酰胺为受体的转糖基化反应。
