Fontés M
Biochimie. 1976;58(10):1155-8. doi: 10.1016/s0300-9084(76)80113-7.
Acid phosphatase (EC. 3.1.3.2) has been separated by molecular sieving into two fractions and these fractions were purified by Sephadex ion-exchange chromatography. One of the purified enzymes (fraction II) was purified 830 fold and had a specific activity of 34 international units per mg protein at 37 degrees C and at a pH of 4.9. The Km value with p-nitrophenylphosphate as substrate was 9.10(-4) M and the kinetic studies showed no possibilities of control by allosteric transitions, and no effect of metabolites (amino acids) on the reaction velocity.
酸性磷酸酶（EC. 3.1.3.2）已通过分子筛分离成两个组分，这些组分通过葡聚糖离子交换色谱法进行纯化。其中一种纯化后的酶（组分II）纯化了830倍，在37℃和pH值为4.9时，每毫克蛋白质的比活性为34国际单位。以对硝基苯磷酸酯为底物时的米氏常数为9×10⁻⁴ M，动力学研究表明不存在通过别构转变进行调控的可能性，并且代谢物（氨基酸）对反应速度没有影响。
