The oligomycin-sensitive ADP-ATP exchange of intact mitoplasts (inner membrane + matrix particles) of rat liver mitochondria is inhibited less than 22% by KCN when assayed without added phosphate at either high or low nucleotide concentrations. 32P-ATP formation amounts to less than 35% of the 14C-ATP formed and is almost completely insensitive to KCN. Oxidation of endogenous substrates is inhibited nearly 100% by KCN. It is concluded that net ATP synthesis supported by oxidation of endogenous substrates accounts for only a small fraction of the total 14C-ATP formed in the ADP-ATP exchange assay and that the bulk of this activity is catalyzed independently by the terminal reactions of oxidative phosphorylation.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Nov 5 1971|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology