花生酸性磷酸酶的纯化与特性分析
Purification and characterization of an acid phosphatase from Arachis hypogaea.
作者信息
Srivastava R, Rajput Y S, Khare S K, Tyagi R, Gupta M N
机构信息
Chemistry Department I.I.T. Delhi, India.
出版信息
Biochem Mol Biol Int. 1995 Apr;35(5):949-56.
An acid phosphatase from Arachis hypogaea (peanuts) has been purified. The electrophoretically homogeneous enzyme preparation is free of any phophodiesterase activity. The enzyme has a molecular weight of 120,000. Among the various phosphomonoesters tested, p-nitrophenylphosphate was found to be its most effective substrate. The Km for p-nitrophenylphosphate was 1.21 mM at pH 5.0 and 25 degrees C. The enzyme was thermostable and did not loose activity after 1 hr at 50 degrees C.
已从花生（落花生）中纯化出一种酸性磷酸酶。该电泳纯的酶制剂不含任何磷酸二酯酶活性。该酶的分子量为120,000。在测试的各种磷酸单酯中，对硝基苯磷酸被发现是其最有效的底物。在pH 5.0和25℃下，对硝基苯磷酸的Km为1.21 mM。该酶具有热稳定性，在50℃下1小时后不会丧失活性。
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