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 language | English (US) |
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Pages (from-to) | 1182-1188 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 71 |
Issue number | 4 |
DOIs | |
State | Published - Aug 23 1976 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology