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Contribution of ATP synthesis from endogenous substrates to the oligomycin-sensitive ADP-ATP exchange activity of rat liver mitoplasts

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
45
Issue
3
Identifiers
DOI: 10.1016/0006-291x(71)90489-x

Abstract

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.

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