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- W2003703148 abstract "The 2,4-dinitrophenol-stimulated ATPase activity and the 32P-ATP exchange reaction has been studied in rat liver mitochondria having less than 15 nmoles of K+ per milligram of protein. With 200 mm sucrose in the incubation media, the permeation of K+ and an oxidizable substrate is required for maximal stimulation of ATPase activity by 2,4-dinitrophenol. In these conditions, the 2,4-dinitrophenol-stimulated ATPase is inhibited by antimycin, acetate and mersalyl and depends to a certain extent on the rate of electron transport. The 32P-ATP exchange reaction of mitochondria with a low content of K+ also requires K+ permeation and is inhibited by antimycin, cyanide, 2,4-dinitrophenol, and acetate. The results suggest that the entrance of ATP into the mitochondria is compulsory linked to K+ uptake in a process that depends on a negative internal potential." @default.
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- W2003703148 date "1972-11-01" @default.
- W2003703148 modified "2023-09-26" @default.
- W2003703148 title "Dependency of the ATPase and 32P—ATP exchange reaction of mitochondria on K+ and electron transport" @default.
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- W2003703148 doi "https://doi.org/10.1016/0003-9861(72)90439-0" @default.
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