Cook N D, Cammack R
Eur J Biochem. 1984 Jun 15;141(3):573-7. doi: 10.1111/j.1432-1033.1984.tb08231.x.
The non-ionic detergent lauryl dimethylamine N-oxide (LDAO) has been used to extract the NADH dehydrogenases of Arum maculatum mitochondria. Affinity chromatography on 5'-ADP-Sepharose 4B was used to separate the rotenone-sensitive (complex I) NADH dehydrogenase from the rotenone-insensitive NADH dehydrogenase. An 18-fold purification of the rotenone-insensitive NADH dehydrogenase was achieved. The enzyme is specific for NADH with optimal activity around pH 7.2. The apparent Km for NADH is 28 microM, with dichloroindophenol as acceptor at pH 7.2. The rotenone-insensitive NADH dehydrogenase appears to be a flavoprotein and no iron-sulphur centres were detected by electron spin resonance spectroscopy.
非离子去污剂月桂基二甲基氧化胺（LDAO）已被用于提取海芋线粒体的NADH脱氢酶。利用5'-ADP-琼脂糖4B进行亲和层析，以分离对鱼藤酮敏感的（复合体I）NADH脱氢酶和对鱼藤酮不敏感的NADH脱氢酶。对鱼藤酮不敏感的NADH脱氢酶实现了18倍的纯化。该酶对NADH具有特异性，在pH 7.2左右具有最佳活性。在pH 7.2时，以二氯靛酚作为受体，NADH的表观Km为28 microM。对鱼藤酮不敏感的NADH脱氢酶似乎是一种黄素蛋白，通过电子自旋共振光谱未检测到铁硫中心。
