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

Peter L. Pedersen; William A. Catterall

doi:10.1016/0006-291X(71)90489-X

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

Peter L. Pedersen, William A. Catterall

School of Medicine

Research output: Contribution to journal › Article › peer-review

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)
Pages (from-to)	809-815
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	45
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(71)90489-X
State	Published - Nov 5 1971

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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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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AU - Catterall, William A.

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N2 - 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.

AB - 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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