嗜热四膜虫酸性磷酸化蛋白磷酸酶的纯化及性质
Purification and properties of an acid phosphoprotein phosphatase from Tetrahymena pyriformis.
作者信息
Lougovoi C P, Paterakis A, Kyriakidis D A
机构信息
Laboratory of Biochemistry, Faculty of Chemistry, Aristotelian University of Thessaloniki, Greece.
出版信息
Biochem Int. 1988 Nov;17(5):847-54.
A cytosolic acid phosphoprotein phosphatase was purified by ion exchange (DEAE-Biogel A, DE-52) and hydrophobic (Phenyl-Sepharose) chromatography. The purified phosphoprotein phosphatase was homogeneous as judged by polyacrylamide gel electrophoresis under native or denature conditions. The enzyme has a Mr of 90.000. The Km value and the optimum pH determined with p-nitrophenyl phosphate was 0.3 mM and 4.0, respectively. The enzyme is inhibited by NaF, ATP, 5'-pyridoxal phosphate and slightly activated by divalent cations.
一种胞质酸性磷酸蛋白磷酸酶通过离子交换（DEAE-琼脂糖凝胶A、DE-52）和疏水（苯基琼脂糖）色谱法进行纯化。通过在天然或变性条件下的聚丙烯酰胺凝胶电泳判断，纯化后的磷酸蛋白磷酸酶是均一的。该酶的分子量为90,000。以对硝基苯磷酸酯测定的Km值和最适pH分别为0.3 mM和4.0。该酶受到氟化钠、ATP、5'-磷酸吡哆醛的抑制，并受到二价阳离子的轻微激活。
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