中文摘要：

low-molecular-weight 蛋白质酷氨酸磷酸酶(PTPase ) 在初核质和优核质无所不在地存在并且在生理的活动的规定起重要作用。我们这里在 Escherichia coli 从 Thermus thermophilus HB27 报导活跃、可溶的 PTPase 的表示，纯化和描述。当把 p-nitrophenyl 磷酸盐用作底层时，这 PTPase 有 2.84.8 的一个最佳 pH 范围。热 inactivation 结果显示这酶的高热的稳定性，与 75 年代的最佳温度

英文摘要：

The low-molecular-weight protein tyrosine phospha- tases （PTPase） exist ubiquitously in prokaryotes and eukaryotes and play important roles in the regulation of physiological activities. We report here the expression, purification and characterization of an active and soluble PTPase from Thermus thermophilus HB27 in Escherichia coli. This PTPase has an optimum pH range of 2.8-4.8 when using p-nitrophenyl phosphate as the substrate. The thermal inactivation results indicate a high thermal stability of this enzyme, with the optimum temperature of 75℃ for activity. It can be activated by Mn^2＋, Mg^2＋, Ca^2＋, Ba^2＋, and Ni^2＋, but inhibited by Zn^2＋, Cu^2＋, Cl^-, and SO^2-. These results suggest that this heat-resistant PTPase may play important roles in vivo in the adaptation of the microorganism to extreme temperatures and specific nutritional conditions.