Scherer S, Alpes I, Sadowski H, Böger P
Lehrstuhl für Physiologie und Biochemie der Pflanzen Universität Konstanz, West Germany.
Arch Biochem Biophys. 1988 Nov 15;267(1):228-35. doi: 10.1016/0003-9861(88)90027-6.
The NADPH dehydrogenase of the cyanobacterium Anabaena variabilis was solubilized, purified, and characterized. Activity staining after nondenaturing polyacrylamide gel electrophoresis, kinetics, and immunological characterization led to the conclusion that only one thylakoid-associated NADPH dehydrogenase exists in Anabaena, identical with ferredoxin-NADP+ oxidoreductase (FNR). After sodium dodecyl sulfate-polyacrylamide gel electrophoresis an intense band at 34 kDa and a weak band at 52 kDa were found by immunoblotting with an antibody against Anabaena FNR. Using a cell-free preparation competent of oxidative phosphorylation it was demonstrated that FNR operates as a respiratory NADPH dehydrogenase coupled to cyanide-sensitive oxidative ATP formation.
对多变鱼腥藻的NADPH脱氢酶进行了增溶、纯化及特性鉴定。通过非变性聚丙烯酰胺凝胶电泳后的活性染色、动力学分析及免疫学特性鉴定得出结论:鱼腥藻中仅存在一种与类囊体相关的NADPH脱氢酶,它与铁氧还蛋白-NADP⁺氧化还原酶(FNR)相同。经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳后,用抗鱼腥藻FNR的抗体进行免疫印迹,发现有一条34 kDa的强带和一条52 kDa的弱带。利用能够进行氧化磷酸化的无细胞制剂证明,FNR作为一种呼吸型NADPH脱氢酶发挥作用,与对氰化物敏感的氧化ATP形成偶联。