Results 221 to 230 of about 220,750 (263)

Energy Transduction in H+-ATPase

1981
H+-ATPase (F0·F1) is an ATP-synthesizing enzyme present in almost all cells (for review, Kagawa et al. 1979 b), and it has been found in mitochondria (Penefsky 1979), chloroplasts (McCarty 1979) and prokaryotic plasma membranes (Downie et al. 1979). H+-ATPase was extracted from mitochondria with cholate (Kagawa et al.
Y. Kagawa, N. Sone, T. Hamamoto, M. Futai, S. Ohta, T. Wakabayashi   +5 more
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Vacuolar H+-ATPase—an enzyme for all seasons

Pflügers Archiv - European Journal of Physiology, 2008
The life of every eukaryotic cell depends on the function of vacuolar H(+)-ATPase (V-ATPase). Because of its complexity and its challenging properties, the study of this enzyme has lagged behind that of its close relative, F-ATPase. We now know that V-ATPase is vital for many more physiological and biochemical processes than anticipated when the enzyme
Shai, Saroussi, Nathan, Nelson
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Thallium interaction with the gastric (K, H)-ATPase

The Journal of Membrane Biology, 1981
The gastric (K, H)-ATPase has been shown to catalyze an electroneutral H+ for K+ exchange. Tl+ is able to substitute for K+ as an activating cation in the hydrolytic reaction with an apparent dissociation constant of 90 microM as compared to about 870 microM for K+.
E C, Rabon, G, Sachs
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Physiology and Biochemistry of the Kidney Vacuolar H+-ATPase

Annual Review of Physiology, 1996
Vacuolar H+-ATPases have an essential role in renal hydrogen ion secretion in the proximal tubule, collecting duct, and other segments of the nephron. Control of H+ transport is achieved by variations in the intrinsic properties of the renal H+-ATPases and by several cellular regulatory mechanisms, including redistribution of the enzyme both by ...
S L, Gluck, D M, Underhill, M, Iyori, L S, Holliday, T Y, Kostrominova, B S, Lee   +5 more
openaire   +2 more sources

Kidney Vacuolar H+-ATPase: Physiology and Regulation

Seminars in Nephrology, 2006
The vacuolar H(+)-ATPase is a multisubunit protein consisting of a peripheral catalytic domain (V(1)) that binds and hydrolyzes adenosine triphosphate (ATP) and provides energy to pump H(+) through the transmembrane domain (V(0)) against a large gradient.
Patricia, Valles, Michael S, Lapointe, Jan, Wysocki, Daniel, Batlle   +3 more
openaire   +2 more sources

Interaction of Organotins with a Vacuolar-Type H+-ATPase

Biochemical and Biophysical Research Communications, 1996
Organotin-flavone complexes of 3-hydroxyflavone 3,5,7-trihydroxyflavone (galangin) and 2',3,4',5,7-pentahydroxyflavone (morin) are potent inhibitors of the vacuolar H(+)-translocating ATPase from bovine adrenal chromaffin granules, with K, values around 0.3 microM. The fluorescence of the 3-hydroxyflavone complex is enhanced on binding to the purified,
D K, Apps, L C, Webster
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Vacuolar H+-ATPase Signaling Pathway in Cancer

Current Protein & Peptide Science, 2012
Up-regulated aerobic glycolysis is a hallmark of malignant cancers. Little is understood about the reasons why malignant tumors up-regulate glycolysis and acidify their microenvironment. Signaling pathways involved in glucose changes are numerous. However, the identity of the internal glucose signal remains obscure.
Souad R, Sennoune, Raul, Martinez-Zaguilan   +1 more
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Immunocytochemistry of renal H-ATPase.

Mineral and electrolyte metabolism, 1997
In this review we present immunolocalization studies using a monoclonal antibody raised against the 31-kD subunit of bovine H-ATPase, and indirect immunofluorescent staining. In the proximal tubules there is intense H-ATPase staining in the brush borders of S1 and S2, and linear subvillar invagination staining in S1, S2, and S3 segments.
B, Bastani, L, Haragsim
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Vacuolar H(+)-ATPase in the kidney.

Journal of nephrology, 2002
Proton-translocating vacuolar ATPases (H+V-ATPase) are increasingly recognized as essential components of most eukaryotic cells. This electrogenic transporter is present in the cell membranes of many differentiated cell types and in the membranes of many subcellular organelles.
Nazih L, Nakhoul, L Lee, Hamm
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Biosynthesis and Regulation of the Yeast Vacuolar H+-ATPase

Journal of Bioenergetics and Biomembranes, 1999
The yeast V-ATPase is highly similar to V-ATPases of higher organisms and has proved to be a biochemically and genetically accessible model for many aspects of V-ATPase function. Like other V-ATPases, the yeast enzyme consists of a complex of peripheral membrane proteins, the V1 sector, attached to a complex of integral membrane subunits, the V0 sector.
openaire   +2 more sources