大豆磷酸烯醇式丙酮酸磷酸酯酶(PEPP)研究:Ⅱ.纯化与特性  

Studies on soybean phosphoenolpyruvate phosphatase(PEPP):Ⅱ.Purification and characterization

作　　者：董登峰[1] 江立庚[1] 杨杰[1] 陈念平[1] 

机构地区：[1]广西大学农学院,广西南宁530005

出　　处：《广西农业生物科学》2005年第3期225-229,共5页Journal of Guangxi Agricultural and Biological Science

基　　金：广西大学博士启动基金(DD160008)

摘　　要：从大豆叶片中分离磷酸烯醇式丙酮酸磷酸酯酶(phosphoenolpyruvate phosphatase,PEPP),通过硫酸胺分部(20%～50%饱和度)沉淀、DEAE-纤维素层析、羟基磷灰石层析将酶纯化了96.81倍,酶活性达17.91 U/mg蛋白.该酶专一性较强,米氏常数(Km)为0.39 mmol/L(PEP),最适pH 6.8,在pH6.0～7.4范围内及50℃以下较稳定,被Mg2+、Mn2+激活,F-、Cu2+、Zn2+、PO43+、MoO42-抑制.A phosphatase had been isolated from soybean leaves and purified 96.81 folds final sp 50% ecific activity of 17.91 U/mg proteins, through ammonium sulfate fraction precipbation saturation）, DEAE-cellulose chromatography and hydroxyapatite chromatography. This enzyme had high specificity for substrate of phosphoenolpyruvate （PEP）; its Km was 0.39 mmol/L and optimum pH was 6.8. It was relatively stable at the pH ranging from 6.0 to 7.4 and at temperature below 50℃. The enzyme activity was activated by Mg^2＋, Mn^2＋ and inhibited by F^-,Cu^2＋,Zn^2＋,PO^3-,MoO4^2-.

关 键 词：大豆 磷酸烯醇式丙酮酸磷酸酯酶 纯化 特性 

分 类 号：S565.1[农业科学—作物学]