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Kinetics of Inhibition of Polyphenol Oxidase Obtained from Tobacco Nicotiana Tobacum
作者姓名:刘卫群  饶学明  潘继承  周海梦
作者单位:[1]CollegeofAgronomy,HenanAgriculturalUniversity,Zhengzhou450002,China [2]DepartmentofBiologicalSciencesandBiotechnology,TsinghuaUniversity,Beijing100084,China
基金项目:the National Key Basic Research and Develop-ment (973) Program of China (No. G1999075607) and the Henan Natural Science Foundation (No. G0111010700)
摘    要:In this study, the kinetics of inhibition of polyphenol oxidase by L-cysteine has been investigated. The inhibition of tobacco polyphenol oxidase was studied using the progress-of-substrate-reaction method proposed by Tsou, following the substrate reaction during irreversible inhibition of the enzyme activity. Analysis of the inhibition kinetics shows that inhibition occurs by an irreversible and non-complexation reaction. The microscopic rate constants were determined for reaction of the inhibitor both with the free enzyme and with the enzyme-substrate complex. The results show that the presence of the substrate has a significant protective effect of the enzyme against inactivation by L-cysteine.

关 键 词:动力学  多酚氧化酶  烟草  L-半胱氨酸  PPOs

Kinetics of Inhibition of Polyphenol Oxidase Obtained from Tobacco Nicotiana Tobacum
LIU Weiqun ,RAO Xueming,PAN Jicheng ?ZHOU Haimeng College of Agronomy,Henan Agricultural University,Zhengzhou ,China.Kinetics of Inhibition of Polyphenol Oxidase Obtained from Tobacco Nicotiana Tobacum[J].Tsinghua Science and Technology,2004,9(1):94-97.
Authors:LIU Weiqun  RAO Xueming  PAN Jicheng ?ZHOU Haimeng College of Agronomy  Henan Agricultural University  Zhengzhou  China
Abstract:In this study, the kinetics of inhibition of polyphenol oxidase by L-cysteine has been investigated. The inhibition of tobacco polyphenol oxidase was studied using the progress-of-substrate-reaction method proposed by Tsou, following the substrate reaction during irreversible inhibition of the enzyme activity. Analysis of the inhibition kinetics shows that inhibition occurs by an irreversible and non-complexation reaction. The microscopic rate constants were determined for reaction of the inhibitor both with the free enzyme and with the enzyme-substrate complex. The results show that the presence of the substrate has a significant protective effect of the enzyme against inactivation by L-cysteine.
Keywords:tobacco  polyphenol oxidase  kinetics  irreversible inhibition
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