Eisenberg R C, Yu L, Wolin M J
J Bacteriol. 1970 Apr;102(1):172-7. doi: 10.1128/jb.102.1.172-177.1970.
After treating Bacillus megaterium KM membranes with 0.2% sodium deoxycholate, most of the membrane reduced nicotinamide adenine dinucleotide (NADH) oxidase was inactivated, and all of the membrane NADH-2,6 dichlorophenol indophenol oxidoreductase was solubilized. Dilution of the deoxycholate-treated membranes in the presence of divalent cations restored almost all of the original membrane NADH oxidase. The effectiveness of the divalent cation activation decreased in the order Ba(2+) > Ca(2+) > Mg(2+) > Mn(2+). After centrifugation, the deoxycholate-treated membranes at 100,000 x g for 1 hr, all of the NADH oxidase that was activated by a divalent cation was soluble. Cation-activated oxidase, however, was insoluble. The results show that 0.2% deoxycholate at least partially solubilizes the total electron chain from NADH to O(2) in an inactive from which can be reactivated by divalent cations with the formation of active, insoluble NADH oxidase.
用0.2%脱氧胆酸钠处理巨大芽孢杆菌KM膜后，大部分膜还原型烟酰胺腺嘌呤二核苷酸（NADH）氧化酶失活，且所有膜NADH - 2,6 - 二氯酚靛酚氧化还原酶都被溶解。在二价阳离子存在的情况下稀释经脱氧胆酸钠处理的膜，几乎可恢复所有原始膜NADH氧化酶的活性。二价阳离子激活的有效性按Ba(2+) > Ca(2+) > Mg(2+) > Mn(2+)的顺序降低。经100,000×g离心处理1小时后的经脱氧胆酸钠处理的膜，所有被二价阳离子激活的NADH氧化酶都是可溶的。然而，阳离子激活的氧化酶是不溶的。结果表明，0.2%脱氧胆酸钠至少部分溶解了从NADH到O(2)的总电子传递链，使其处于无活性状态，这种无活性状态可被二价阳离子重新激活，形成有活性的、不溶的NADH氧化酶。
