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) |
|---|---|
| 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 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Adenosine triphosphatase from rat liver mitochondria - Evidence for a mercurial-sensitive site for the activating anion bicarbonate. / Pedersen, Peter L.
In: Biochemical and Biophysical Research Communications, Vol. 71, No. 4, 23.08.1976, p. 1182-1188.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Adenosine triphosphatase from rat liver mitochondria - Evidence for a mercurial-sensitive site for the activating anion bicarbonate
AU - Pedersen, Peter L
PY - 1976/8/23
Y1 - 1976/8/23
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.
UR - http://www.scopus.com/inward/record.url?scp=0017066277&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017066277&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(76)90778-6
DO - 10.1016/0006-291X(76)90778-6
M3 - Article
C2 - 135559
AN - SCOPUS:0017066277
VL - 71
SP - 1182
EP - 1188
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -