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Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle.

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TLDR
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.
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This article is published in Journal of Biological Chemistry.The article was published on 1977-11-10 and is currently open access. It has received 815 citations till now. The article focuses on the topics: Vanadate & Sodium orthovanadate.

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Journal ArticleDOI

Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate.

TL;DR: Results show that vanadate is a potent and selective inhibitor of phosphotyrosyl-protein phosphatase.
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Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps.

TL;DR: These properties are consistent with an enzyme in which the equilibrium between the E1 and E2 conformations is shifted toward the E2 state.
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Cyclin activation of p34cdc2

TL;DR: The concerted transition into mitosis involves both a reduction in the rate of p34cdc2 phosphorylation on tyrosine and an increase in its rate of dephosphorylation.
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A circulating inhibitor of (Na+ + K+) ATPase associated with essential hypertension

TL;DR: A highly significant correlation is demonstrated between levels of a plasma inhibitor of (Na+ + K+)ATPase activity and mean arterial blood pressure in normotensive and hypertensive individuals, providing evidence for the involvement of a circulating Na+ pump inhibitor in the genesis of essential hypertension.
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Insulin-like stimulation of glucose oxidation in rat adipocytes by vanadyl (IV) ions

TL;DR: Externally applied vanadate ions at low concentrations mimic fully the effect of insulin on glucose oxidation in rat adipocytes, however, this simulation seems to be due mainly to the effects of vandyl (IV) ions, probably produced within the cells, and not primarily to inhibition of the sodium pump.
References
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Journal ArticleDOI

Purification and characterization of (Na+ + K+)-ATPase III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate

TL;DR: Analysis of the protein composition by sodium dodecylsulphate gel electrophoresis and determination of the capacities for binding of ATP and ouabain and for sodium-dependent phosphorylation show that the procedures lead to a true purification of the enzyme.
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Vanadium ion inhibition of alkaline phosphatase-catalyzed phosphate ester hydrolysis

TL;DR: Observations indicate that VO3− can bind quite specifically at the phosphate-binding site on the enzyme, which suggests that the enzyme-complexed inhibitor may have some resemblance to the metastable intermediate formed during the hydrolysis of phosphate esters.
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