Results 261 to 270 of about 238,289 (304)

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
openaire   +1 more source

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
openaire   +1 more source

Biogenesis of the yeast vacuolar H+-ATPase

Journal of Experimental Biology, 1992
ABSTRACT Achieving an understanding of the biosynthesis, assembly and intracellular targeting of the vacuolar H+-ATPase is critical for understanding the distribution of acidic compartments and the regulation of organelle acidification.
openaire   +2 more sources

[H+, K+ -ATPase, H+ -ATPase].

Nihon rinsho. Japanese journal of clinical medicine, 1997
Gastric H+, K+ -ATPase comprised of alpha- and beta-subunits was functionally expressed in an animal cell-line. When glutamic acid (345) of the alpha-subunit was mutated to glutamine, the affinity of K+ decreased 10-fold, indicating that this residue in the 4th transmembrane domain engages in the determination of the K+ affinity.
N, Takeguchi, S, Asano, M, Morii
openaire   +1 more source

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
openaire   +2 more sources

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
openaire   +2 more sources

Vacuolar H+-ATPase Signaling in Cancer

2015
The vacuolar H+-ATPase (V-ATPase) is an electrogenic H+ pump responsible for the regulation of pH in endomembranous compartments; and for the extrusion of H+ across the plasma membrane in certain cell types, including metastatic cells. The study of the regulation of V-ATPase has been daunting.
Raul Martínez-Zaguilán, Souad R. Sennoune   +1 more
openaire   +1 more source

Studies on (K+ + H+)-ATPase

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1981
F.J.M. van de Ven, J.J. Schrijen, J.J.H.H.M. de Pont, S.L. Bonting   +3 more
openaire   +2 more sources

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
openaire   +1 more source

Vacuolar H+-ATPase Assembly

2014
Anne Smardon, Patricia Kane
openaire   +2 more sources