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• W2049043357 startingPage "569" @default.
• W2049043357 abstract "Human tissues contain at least two enzymes capable of releasing glucose from 4-methylumbelliferyl-β-d-glucopyranoside, but only one of these enzymes can hydrolyze glucocerebroside and is deficient in individuals with Gaucher's disease. In the present report, we demonstrate that, in human liver, these two β-glucosidases differ in terms of their subcellular localization, chromatographic behavior on ion-exchange columns, substrate specificity, and sensitivity to inhibition or activation by sodium taurocholate and phospholipids. We also demonstrate that when the relatively nonspecific, artificial β-glucoside substrate, 4-methylumbelliferyl-β-d-glucopyranoside, is used under assay conditions optimal for glucocerebroside hydrolysis, it is effective in measuring relative glucocerebroside:β-glucosidase activity and can be used to evaluate an individual's status with respect to Gaucher's disease. These conditions of assay require a pH near neutrality (pH 5.5–6.5) and the presence of the detergent sodium taurocholate. The inclusion of sodium taurocholate in assays using 4-methylumbelliferyl-β-d-glucopyranoside as substrate permits the specific measurement of glucocerebroside:β-glucosidase activity because sodium taurocholate inhibits the nonspecific β-glucosidase not involved in Gaucher's disease and stimulates the relevant β-glucocerebrosidase activity." @default.
• W2049043357 created "2016-06-24" @default.
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• W2049043357 date "1976-08-01" @default.
• W2049043357 modified "2023-09-27" @default.
• W2049043357 title "Differentiation of β-glucocerebrosidase from β-glucosidase in human tissues using sodium taurocholate" @default.
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• W2049043357 doi "https://doi.org/10.1016/0003-9861(76)90547-6" @default.
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