Biochemical Properties and Inhibition Kinetics of Phosphatase from Wheat Thylakoid Membranes
Biochemical Properties and Inhibition Kinetics of Phosphatase from Wheat Thylakoid Membranes作者机构：College of Life Sciences Shandong Agricultural University Taian 271018 China Shandong Key Laboratory of Crop Biology Shandong Agricultural University Taian 271018 China
出 版 物：《Journal of Integrative Plant Biology》 (植物学报（英文版）)
年 卷 期：2006年第48卷第3期
页 面：294-299页
核心收录：
基 金：国家973计划
主 题：calcium ions copper enzyme activity enzyme inhibitors enzymes ethanol ferric ions fluoride glycols ions kinetics magnesium manganese methanol molybdates phosphate phosphoric monoester hydrolases solvents thylakoids wh eat
摘 要：A phosphetase that hydrolyses phosphate monoesters has been Isolated from wheat thylakold membranes. Biochemical properties and inhibition kinetics of the phosphatase were Investigated using several Ions, organlc solvents, and Inhlbltors. Wheat （Trltlcum aestivum L. cv. PH82-2-2） thylakold membrane phosphatase activity was activated by Mg^2＋, Ca^2＋, and Fe^2＋ and was inhibited by Mn^2＋ and Cu^2＋. For example, enzyme activity was acUvated 34.81% by 2 mmol/l. Mg^2＋, but was Inhibited 22.3% and 8.5% by 2 and 1 mmol/L Cu^2＋, respectively. Methanol, ethanol and glycol were all able to activate enzyme activity. Enzyme activity was activated 58.5%, 48.2%, and 8.7% by 40% ethanol, methanol and glycol, respectively. From these results, It can be seen that the degree of actlvetlon of the phosphetase was greatest for ethanol and the type of acUvatlon was uncompetltlve. Moreover, the activity of the thylakold membrane phosphetase was Inhibited by molybdate, vanadete, phosphate, and fluoride and the type of Inhibition produced by these elements was uncompetltlve, non-competitive, competltlve and mixed, respectively.
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