Zecher R, Wolf H U
Biochem J. 1980 Oct 1;191(1):117-24. doi: 10.1042/bj1910117.
Human erythrocytes contain a phosphatase that is highly specific for phosphoglycollate. It shows optimum pH of 6.7 and has Km 1 mM for phosphoglycollate. The molecular weight appears to be about 72000. The enzyme is a dimeric molecule having subunits of mol. wt. about 35000. It could be purified approx. 4000-fold up to a specific activity of 5.98 units/mg of protein. The activity of the enzyme is Mg2+-dependent. Co2+, and to a smaller extent Mn2+, may substitute for Mg2+. Half-maximum inhibition of the phosphatase by 5,5'-dithiobis-(2-nitrobenzoate), EDTA and NaF is obtained at 0.5 microM, 1 mM and 4 mM respectively. Moreover, it needs a univalent cation for optimum activity. Phosphoglycollate phosphatase is a cytoplasmic enzyme. Approx. 5% of its total activity is membrane-associated. This part of activity can be approx. 70% solubilized by freezing, thawing and treatment with 0.25% Triton X-100.
人类红细胞含有一种对磷酸乙醇酸具有高度特异性的磷酸酶。它的最适pH为6.7,对磷酸乙醇酸的Km值为1 mM。分子量约为72000。该酶是一种二聚体分子,其亚基分子量约为35000。它可以被纯化约4000倍,达到比活性为5.98单位/毫克蛋白质。该酶的活性依赖于Mg2+。Co2+以及在较小程度上的Mn2+可以替代Mg2+。5,5'-二硫代双(2-硝基苯甲酸)、EDTA和NaF对磷酸酶的半最大抑制浓度分别为0.5 microM、1 mM和4 mM。此外,它需要一价阳离子来达到最佳活性。磷酸乙醇酸磷酸酶是一种细胞质酶。其总活性的约5%与膜相关。这部分活性可以通过冷冻、解冻和用0.25% Triton X-100处理而约70%溶解。