Kinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by sodium (2,2'-bipyridine) oxodiperoxovanadate |
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Authors: | Zhou X W Zhuang Z L Chen Q X |
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Affiliation: | (1) Department of Biology, Xiamen University, Xiamen, 361005, P. R. China |
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Abstract: | Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme, which catalyzes the nonspecific hydrolysis of phosphate monoesters. The kinetics of inhibition of the enzyme by sodium (2, 2-bipyridine) oxodiperoxovanadate, pV(bipy), has been studied. The time course of the hydrolysis of p-nitrophenyl-phosphate catalyzed by the enzyme in the presence of different pV(bipy) concentrations showed that at each pV(bipy) concentration, the rate decreased with increasing time until a straight line was approached, the straight line slopes are the same for all concentrations. The results suggest that the inhibition of the enzyme by pV(bipy) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined for the reaction of inhibitor with the enzyme. |
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Keywords: | Alkaline phosphatase sodium (2, 2 /content/w5k4743763047h46/xxlarge8242.gif" alt=" prime" align=" BASELINE" BORDER=" 0" >-bipyridine) oxodiperoxovanadate inhibition kinetics |
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