Abstract
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) |
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Pages (from-to) | 809-815 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 45 |
Issue number | 3 |
DOIs | |
State | Published - Nov 5 1971 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology