Properties of β-Glucuronidase Bound to p-Aminophenyl 1-Thio-β-D-glucopyranosiduronic Acid-CH-Sepharose 4B
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概要
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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 K_m 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.
- 社団法人日本薬学会の論文
- 1984-09-25
著者
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吉田 和夫
Daiichi College Of Pharmaceutical Sciences
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飯野 信子
Daiichi College of Pharmaceutical Sciences
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吉富 美起
Daiichi College of Pharmaceutical Sciences
関連論文
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