枯草芽孢杆菌BS12乳酸脱氢酶的分离纯化与部分性质的研究  

Purification and Some Properties of Lactate Dehydrogenase from Bacillus subtilis BS12

作　　者：朱文淼[1] 肖敏[1] 刘复今 

机构地区：[1]山东医科大学微生物教研室,山东大学微生物系

出　　处：《生物技术》1996年第2期23-25,共3页Biotechnology

摘　　要：枯草芽孢杆菌ＢＳ１２的乳酸脱氢酶经硫酸铵分级沉淀、ＣＭ－纤维素、ＤＥＡＥ－纤维素离子交换柱层析、ＳｅｐｈａｄｅｘＧ—２００柱层析，得到了凝胶电脉均一的样品。用ＳＤＳ—ＰＡＧＥ测得其亚基分子量为２８０００Ｄａ。酶反应的最适ｐＨ为７．０，最适温度为３５℃。Lactate dehydrogenase(LDH. EC1.1.1.27)from Bacillus subtilis BS12 was purified to electrophoretic homogeneity by ammonium sulfate fractionation,CM-cellulose DEAE cellulose ionexchange chromatography and Sephadex G200 column chromatography.The enzyme was purified 102. 5 folds with 23. 2% recovey of activity. The subunit molecular weight was estimated to be 28000 dations by SDS- polyacrylamide gel electrophoresis.The optimum pH and temperature for enzyme catalysls were 7.0 and 35℃,respectively.

关 键 词：枯草芽孢杆菌 乳酸脱氢酶 分离 提纯 

分 类 号：Q939.124[生物学—微生物学]