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- W4247661623 abstract "Here we report a fast, simple purification for thermophilic F1F0 ATP synthase (TF1F0) that utilizes a cocktail of stabilizing reagents and the detergent n-dodecyl β-d-maltoside to yield enzyme with an ATPase activity of 41 μmol/min/mg, 2.5-fold higher than that previously reported. ATPase activity was 80% inhibited by the F0-reactive reagent dicyclohexylcarbodiimide, indicating that F1–F0 interactions were largely intact. To measure ATP-driven proton pumping activity, purified TF1F0 was incorporated into liposomes, and the ATP-induced change in internal pH was measured using the fluorescent probe pyranine. In the presence of valinomycin, a maximum ATP-driven ΔpH of 0.8 units was obtained. To measure ATP synthesis activity, TF1F0 was incorporated into liposomes with the light-dependent proton pump bacteriorhodopsin. Proteoliposomes were illuminated to generate an electrochemical gradient, after which ADP and inorganic phosphate were added to initiate ATP synthesis. A steady state ATP synthesis activity of 490 nmol/min/mg was achieved after an initial ∼30-min lag phase." @default.
- W4247661623 created "2022-05-12" @default.
- W4247661623 date "2003-05-01" @default.
- W4247661623 modified "2023-10-14" @default.
- W4247661623 title "IFC - Author index" @default.
- W4247661623 doi "https://doi.org/10.1016/s0003-9861(03)00180-2" @default.
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