Yasuura S, Nagaoka I, Yamashita T, Namihisa T
Comp Biochem Physiol B. 1985;82(4):595-8. doi: 10.1016/0305-0491(85)90495-x.
We characterized the bovine polymorphonuclear neutrophil alkaline phosphatase which was considerably purified with a sp. act. of 206 units/mg of protein. The Km value for p-nitrophenylphosphate at pH 10.0 was 1.69 mM. L-Histidine, imidazole and L-homoarginine but not L-phenylalanine inhibited the enzyme. In heat stability study, the enzyme lost 50% activity at 56 degrees C for 20 min. The enzyme had a half-life of 30 min in 3 M urea at 37 degrees C and pH 7.5. The enzyme was inhibited by beta-mercaptoethanol in a dose-dependent fashion. It is suggested from above results that the neutrophil alkaline phosphatase isozyme could be distinguishable from other tissue isozymes.
我们对牛多形核中性粒细胞碱性磷酸酶进行了特性描述，该酶经大量纯化，比活性为206单位/毫克蛋白质。在pH 10.0时，对硝基苯磷酸酯的Km值为1.69 mM。L-组氨酸、咪唑和L-高精氨酸可抑制该酶，而L-苯丙氨酸则无此作用。在热稳定性研究中，该酶在56℃下20分钟失去50%的活性。在37℃和pH 7.5的3 M尿素中，该酶的半衰期为30分钟。β-巯基乙醇以剂量依赖方式抑制该酶。从上述结果表明，中性粒细胞碱性磷酸酶同工酶可与其他组织同工酶区分开来。
