Harsanyi Z, Dorn G L
J Bacteriol. 1972 Apr;110(1):246-55. doi: 10.1128/jb.110.1.246-255.1972.
Acid phosphatase V of Aspergillus nidulans was purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. The enzyme demonstrated a charge microheterogeneity on starch and acrylamide gel electrophoresis, but proved to be homogeneous on ultracentrifugation and gel filtration. Phosphatase V was found to be a classic acid orthophosphoric monoester phosphohydrolase, and it cleaved p-nitrophenylphosphate, glucose-6-phosphate, and uridine-5'-monophosphate at maximal rates. It was inhibited by fluoride, borate, and molybdate ions, and demonstrated end-product inhibition by inorganic phosphate. Metallic ions or cofactors were not required for activity. The molecular weight was estimated to be 100,000, the S(20,w) was calculated to be 4.1, and the pH optimum was found to be 6.1.
通过硫酸铵沉淀、凝胶过滤和离子交换色谱法对构巢曲霉的酸性磷酸酶V进行了纯化。该酶在淀粉和丙烯酰胺凝胶电泳上表现出电荷微不均一性，但在超速离心和凝胶过滤中被证明是均一的。发现磷酸酶V是一种典型的酸性正磷酸单酯磷酸水解酶，它能以最大速率切割对硝基苯磷酸酯、葡萄糖-6-磷酸酯和尿苷-5'-单磷酸酯。它受到氟化物、硼酸盐和钼酸盐离子的抑制，并表现出无机磷酸盐的终产物抑制作用。活性不需要金属离子或辅因子。估计分子量为100,000，计算出的S(20,w)为4.1，发现最适pH为6.1。
