Journal ArticleDOI
Vanadate inhibition of sarcoplasmic reticulum Ca2+-ATPase and other ATPases.
TLDR
Vanadate is a potent inhibitor of the Ca2+-ATPase activity of sarcoplasmic reticulum in the presence of A-23187 and the purified enzyme is sensitive to vanadate even in the absence of the ionophore.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1979-08-13. It has received 213 citations till now. The article focuses on the topics: Vanadate & ATPase.read more
Citations
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Journal ArticleDOI
Regulation and Modulation of pH in the Brain
TL;DR: The regulation of pH is a vital homeostatic function shared by all tissues, and mechanisms responsible for the regulation of intracellular pH in brain are similar to those of other tissues, but differences in the expression or efficacy of these mechanisms have been noted among the functionally and morphologically diverse neurons and glial cells that have been studied.
Journal ArticleDOI
Effect of Vanadate, Molybdate, and Azide on Membrane-Associated ATPase and Soluble Phosphatase Activities of Corn Roots
TL;DR: While vanadate does not appear to be a selective inhibitor, it can be used in combination with molybdate and azide to distinguish the plasma membrane ATPase from mitochondrial ATPase or supernatant acid phosphatase.
Journal ArticleDOI
Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence.
TL;DR: Results provide evidence for the presence of an electrogenic proton pump driven by MgATP (H+-ATPase) on lysosomes.
Journal ArticleDOI
Golgi membranes contain an electrogenic H+ pump in parallel to a chloride conductance.
TL;DR: It is demonstrated that Golgi vesicles can form a pH difference and a membrane potential through the action of an electrogenic proton translocating ATPase.
Journal ArticleDOI
Vanadium — an element in search of a role
TL;DR: Vanadium has recently begun to interest the biochemist, largely as a result of the discovery that it can act as a potent inhibitor of the sodium pump as mentioned in this paper. But vanadium's biological functions remain unknown.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI
Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle.
TL;DR: A potent (Na,K)-ATPase inhibitor purified from "Sigma Grade* ATP" has been identified as vanadium using electron probe microanalysis and confirmed by microwave-induced emission spectroscopy and electron paramagnetic resonanceSpectroscopy.
Journal ArticleDOI
Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum
TL;DR: An adenosine triphosphatase has been purified approximately 6-fold from sarcoplasmic reticulum through the use of deoxycholate and salt fractionation and the rate of ATP-ADP exchange and the level of phosphorylation are both increased by a factor commensurate with the increase in ATPase activity.
Journal ArticleDOI
A characterization of vanadate interactions with the (Na,K)-ATPase. Mechanistic and regulatory implications.
TL;DR: The interaction of vanadium in the +5 oxidation state (vanadate) with purified dog kidney Na+ and K+-stim- ulated adenosine trlphosphatase [(Na,K)-ATPase] has been studied using equilibrium binding, steady state kinetics, and measurements of relaxation kinetics.
A Characterization of Vanadate Interactions with the (Na,K)-ATPase
TL;DR: The interaction of vanadium in the +5 oxidation state (vanadate) with purified dog kidney Na+ and K+-stim- ulated adenosine trlphosphatase [(Na,K)-ATPase] has been studied using equilibrium binding, steady state kinetics, and measurements of relaxation kinetics as discussed by the authors.