Hy M, Reeves H C
Biochim Biophys Acta. 1976 Sep 14;445(2):280-5. doi: 10.1016/0005-2744(76)90082-6.
The NADP+-specific isocitrate dehydrogenase (threo-DS-isocitrate:NADP+ oxidoreductase (decarboxylating), EC 1.1.1.42) of Excherichia coli has been purified to electrophoretic homogeneity by a two-step purification procedure employing affinity chromatography. The overall yield of enzyme was 30% with specific activity 125 mumol/min per ng protein. Electrophoretic homogeneity of the isocitrate dehydrogenase was deterimed in analytical polyacrylamide gels in a Tris/acetate/EDTA buffer system at pH 7.5 and in a citrate/phosphate buffer system at pH 6.0.
利用亲和层析两步纯化程序，已将大肠杆菌的NADP⁺特异性异柠檬酸脱氢酶（苏糖-DS-异柠檬酸：NADP⁺氧化还原酶（脱羧），EC 1.1.1.42）纯化至电泳纯。酶的总产率为30%，比活性为每纳克蛋白质125微摩尔/分钟。在pH 7.5的Tris/醋酸盐/EDTA缓冲系统和pH 6.0的柠檬酸盐/磷酸盐缓冲系统中的分析型聚丙烯酰胺凝胶中测定异柠檬酸脱氢酶的电泳纯度。
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