Douglas M G, Koh Y, Dockter M E, Schatz G
J Biol Chem. 1977 Dec 10;252(23):8333-5.
Isolated beta subunit of ATPase (F1) from yeast mitochondria does not catalyze an ATPase reaction but still binds the specific F1 inhibitor aurovertin. Binding was measured by enhancement of aurovertin fluorescence; it was as tight as that to F1-ATPase. No binding was observed with F1 or with isolated beta subunit from a single-gene nuclear yeast mutant whose F1-ATPase was resistant to aurovertin.
从酵母线粒体中分离出的ATP酶(F1)的β亚基不催化ATP酶反应,但仍能结合特异性F1抑制剂金褐霉素。通过金褐霉素荧光增强来测定结合情况;其结合紧密程度与F1-ATP酶相同。对于F1或来自单基因核酵母突变体的分离β亚基,未观察到结合,该突变体的F1-ATP酶对金褐霉素具有抗性。