Dmitriev O Iu, Dann S, Krasnosel'skaia I A, Papa S, Skulachev V P
Biokhimiia. 1992 Oct;57(10):1499-507.
F0F1-ATPase has been isolated from the marine alkali-resistant bacterium Vibrio alginolyticus. The enzyme subunits cross-reacted with antibodies against subunits alpha, beta, gamma, epsilon, and b of E. coli ATPase. The purified ATPase was reconstituted into liposomes effecting an ATP-dependent uptake of H+. Proton transport was inhibited by the ATPase blockers DCCD, triphenyltin, and venturicidin. Na+ ions had no effect on ATP-dependent proton transport. No ATP-dependent transport of Na+ was detected in proteoliposomes.
已从海洋耐碱细菌溶藻弧菌中分离出F0F1 - ATP酶。该酶亚基与抗大肠杆菌ATP酶α、β、γ、ε和b亚基的抗体发生交叉反应。纯化的ATP酶被重组到脂质体中,实现了ATP依赖的H⁺摄取。ATP酶阻滞剂二环己基碳二亚胺(DCCD)、三苯基锡和抗霉素A抑制质子转运。Na⁺离子对ATP依赖的质子转运没有影响。在蛋白脂质体中未检测到ATP依赖的Na⁺转运。