Results 301 to 310 of about 13,532,360 (331)
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Thermal stability of soluble mitochondrial H+-ATPase
Biophysics of Structure and Mechanism, 1979ATPase melting has been studied by circular dichroism and differential scanning microcalorimetry. Decomposition of the alpha-helix of H+-ATPase (in which about 80% of the peptide groups of the enzyme are involved) following thermal treatment is shown to proceed gradually, beginning with room temperature.
A A, Kiladze +3 more
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Cellular physiology of the renal H+ATPase
Current Opinion in Nephrology and Hypertension, 2009Vacuolar-type H+ATPases are multisubunit macromolecules that play an essential role in renal acid-base homeostasis. Other cellular processes also rely on the proton pumping ability of H+ATPases to acidify organellar or lumenal spaces. Several diseases, including distal renal tubular acidosis, osteoporosis and wrinkly skin syndrome, are due to mutations
Katherine G, Blake-Palmer +1 more
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2014
Vacuolar H+-ATPase Assembly Structure of Prokaryotic V type ATPase/synthase The function of V-ATPase in the degradation of gluconeogenic enzymes in the yeast vacuole The Role of Vacuolar ATPase in the Regulation of Npt2a Trafficking Cytosolic pH regulated by glucose promotes V-ATPase assembly Vacuolar H+-ATPase (V-ATPase) activated by glucose, a ...
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Vacuolar H+-ATPase Assembly Structure of Prokaryotic V type ATPase/synthase The function of V-ATPase in the degradation of gluconeogenic enzymes in the yeast vacuole The Role of Vacuolar ATPase in the Regulation of Npt2a Trafficking Cytosolic pH regulated by glucose promotes V-ATPase assembly Vacuolar H+-ATPase (V-ATPase) activated by glucose, a ...
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Energy Transduction in H+-ATPase
1981H+-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 +5 more
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Immunocytochemistry of renal H-ATPase.
Mineral and electrolyte metabolism, 1997In 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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Biogenesis of the yeast vacuolar H+-ATPase
Journal of Experimental Biology, 1992ABSTRACT 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.
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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
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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
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Vacuolar H+-ATPase—an enzyme for all seasons
Pflügers Archiv - European Journal of Physiology, 2008The 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, 1981The 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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