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- W2317251156 abstract "β-Glucuronidase [EC 3. 2. 1. 31] from bovine liver was bound to the adsorbent prepared by coupling p-aminophenyl 1-thio-β-D-glucopyranosiduronic acid with CH-Sepharose 4B. The properties of the immobilized β-glucuronidase were studied in comparison with those of the soluble enzyme. The inhibition of immobilized β-glucuronidase by saccharo-1, 4-lactone is slightly lower than that of the soluble enzyme. The pH-activity profile for the immobilized enzyme is similar to that for the soluble enzyme. The Km values of the soluble enzyme for p-nitrophenyl β-D-glucopyranosiduronic acid, estriol-3-β-D-glucopyranosiduronic acid and estriol-16α-β-D-glucopyranosiduronic acid were 0.94, 0.25 and 6.6mM, respectively, and these values did not change significantly in the immobilized form. The immobilized enzyme retained 66% of its initial activity after storage for 6 months." @default.
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- W2317251156 date "1984-01-01" @default.
- W2317251156 modified "2023-09-25" @default.
- W2317251156 title "Properties of .BETA.-glucuronidase bound to p-aminophenyl 1-thio-.BETA.-D-glucopyranosiduronic acid-CH-sepharose 4B." @default.
- W2317251156 doi "https://doi.org/10.1248/cpb.32.3710" @default.
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