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

Journal Article · Mon Aug 23 00:00:00 EDT 1976 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(76)90778-6· OSTI ID:7326257

Pedersen, P L

The ATPase activity of purified mitochondrial ATPase (F/sub I/) of rat liver is inhibited less than 15 percent 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 /sup 14/C-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.

• Research Organization: Johns Hopkins Univ., Baltimore
• OSTI ID: 7326257
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 71:4; ISSN BBRCA
• Country of Publication: United States
• Language: English

Related Subjects

550200 -- Biochemistry
560305* -- Chemicals Metabolism & Toxicology-- Vertebrates-- (-1987)
59 BASIC BIOLOGICAL SCIENCES
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ANIMALS
ANIONS
ATP
ATP-ASE
BIOCHEMISTRY
BIOLOGICAL EFFECTS
BODY
CARBON COMPOUNDS
CARBONATES
CATALYSIS
CELL CONSTITUENTS
CHARGED PARTICLES
CHEMISTRY
DIGESTIVE SYSTEM
ENZYME INHIBITORS
ENZYMES
ESTERASES
GLANDS
HYDROLASES
INHIBITION
IONS
LIVER
MAMMALS
MERCURY COMPOUNDS
MITOCHONDRIA
NUCLEOTIDES
ORGANIC COMPOUNDS
ORGANOIDS
ORGANS
OXYGEN COMPOUNDS
PHOSPHATASES
RATS
RODENTS
VERTEBRATES