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

Access to Document

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

Cite this

@article{d540bcdaccd64309966d59d0656fe6b1,

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

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.",

author = "Pedersen, {Peter L.} and Catterall, {William A.}",

year = "1971",

month = nov,

day = "5",

doi = "10.1016/0006-291X(71)90489-X",

language = "English (US)",

volume = "45",

pages = "809--815",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Contribution of ATP synthesis from endogenous substrates to the oligomycin-sensitive ADP-ATP exchange activity of rat liver mitoplasts

AU - Pedersen, Peter L.

AU - Catterall, William A.

PY - 1971/11/5

Y1 - 1971/11/5

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.

UR - http://www.scopus.com/inward/record.url?scp=0015212127&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015212127&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(71)90489-X

DO - 10.1016/0006-291X(71)90489-X

M3 - Article

C2 - 4256848

AN - SCOPUS:0015212127

VL - 45

SP - 809

EP - 815

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this