Adenosine triphosphatase from rat liver mitochondria - Evidence for a mercurial-sensitive site for the activating anion bicarbonate

Peter L Pedersen

Research output: Contribution to journalArticle

Abstract

The ATPase activity of purified mitochondrial ATPase (F1) of rat liver is inhibited less than 15% by sulfhydryl reagents when assayed in TrisCl buffer. In Trisbicarbonate buffer the ATPase activity of the enzyme is two- to three-fold higher than in TrisCl. Significantly, the ATPase activity stimulated by bicarbonate can be inhibited by mercurial agents such as p-chloromercuribenzoate. The number of sulfhydryl groups accessible to 14C-p-chloromercuribenzoate is the same in TrisCl and Trisbicarbonate buffers. These experiments suggest that mercurials most likely inhibit bicarbonate-stimulated ATPase activity by blocking a site associated with bicarbonate binding rather than by blocking distinct sulfhydryl-sensitive hydrolytic sites induced by bicarbonate.

Original languageEnglish (US)
Pages (from-to)1182-1188
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume71
Issue number4
DOIs
StatePublished - Aug 23 1976

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Mitochondria
Liver Mitochondrion
Bicarbonates
Liver
Chloromercuribenzoates
Anions
Adenosine Triphosphatases
Rats
Buffers
Sulfhydryl Reagents
Proton-Translocating ATPases
Enzymes
Experiments

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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abstract = "The ATPase activity of purified mitochondrial ATPase (F1) of rat liver is inhibited less than 15{\%} by sulfhydryl reagents when assayed in TrisCl buffer. In Trisbicarbonate buffer the ATPase activity of the enzyme is two- to three-fold higher than in TrisCl. Significantly, the ATPase activity stimulated by bicarbonate can be inhibited by mercurial agents such as p-chloromercuribenzoate. The number of sulfhydryl groups accessible to 14C-p-chloromercuribenzoate is the same in TrisCl and Trisbicarbonate buffers. These experiments suggest that mercurials most likely inhibit bicarbonate-stimulated ATPase activity by blocking a site associated with bicarbonate binding rather than by blocking distinct sulfhydryl-sensitive hydrolytic sites induced by bicarbonate.",
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N2 - The ATPase activity of purified mitochondrial ATPase (F1) of rat liver is inhibited less than 15% by sulfhydryl reagents when assayed in TrisCl buffer. In Trisbicarbonate buffer the ATPase activity of the enzyme is two- to three-fold higher than in TrisCl. Significantly, the ATPase activity stimulated by bicarbonate can be inhibited by mercurial agents such as p-chloromercuribenzoate. The number of sulfhydryl groups accessible to 14C-p-chloromercuribenzoate is the same in TrisCl and Trisbicarbonate buffers. These experiments suggest that mercurials most likely inhibit bicarbonate-stimulated ATPase activity by blocking a site associated with bicarbonate binding rather than by blocking distinct sulfhydryl-sensitive hydrolytic sites induced by bicarbonate.

AB - The ATPase activity of purified mitochondrial ATPase (F1) of rat liver is inhibited less than 15% by sulfhydryl reagents when assayed in TrisCl buffer. In Trisbicarbonate buffer the ATPase activity of the enzyme is two- to three-fold higher than in TrisCl. Significantly, the ATPase activity stimulated by bicarbonate can be inhibited by mercurial agents such as p-chloromercuribenzoate. The number of sulfhydryl groups accessible to 14C-p-chloromercuribenzoate is the same in TrisCl and Trisbicarbonate buffers. These experiments suggest that mercurials most likely inhibit bicarbonate-stimulated ATPase activity by blocking a site associated with bicarbonate binding rather than by blocking distinct sulfhydryl-sensitive hydrolytic sites induced by bicarbonate.

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