Metabolism of Drugs. XLVI. Behavior of 2-Naphthyl β-D-Glucofuranosiduronic Acid toward β-Glucuronidase.

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2. The kinetics of the hydrolysis of 2-naphthyl β-D-glucofuranosiduronic acid by β-glucuronidase were investigated. The pH optimum of the β-D-glucofuranosiduronic acid is 5.0 in phosphate-citrate buffer at 38°. The reaction velocity is constant with time. The Michaelis-Menten constant is 1.75×10-2M. The kinetics of the hydrolysis of 2-naphthyl β-D-glucopyranosiduronic acid by the enzyme were also investigated. The pH optimum is 4.7. The Michaelis-Menten constant is 1.3×10-3M. 3. In view of the above facts, it was concluded that β-D-glucofuranosiduronic acids could be a substrate for β-glucuronidase.

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