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- W2076174511 abstract "Inhibition of yeast plasma membrane ATPase by vanadate occurs only if either Mg2+ or MgATP2− is bound to the enzyme. The dissociation constant of the complex of vanadate and inhibitory sites is 0.14–0.20 μM in the presence of optimal concentrations of Mg2+ and of the order of 1 μM if the enzyme is saturated with MgATP2−. The dissociation constants of Mg2+ and MgATP2− for the sites involved are 0.4 and 0.62–0.73 mM, respectively, at pH 7. KCl does not increase the affinity of vanadate to the inhibitory sites as was found with (Na+ + K+)-ATPase. On the other hand, the effect of Mg2+ upon vanadate binding is similar to that upon (Na+ + K+)-ATPase, and the corresponding affinity constants of Mg2+ and vanadate for the two enzymes are of the same order of magnitude." @default.
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- W2076174511 date "1981-03-01" @default.
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- W2076174511 title "Factors affecting the inhibition of yeast plasma membrane ATPase by vanadate" @default.
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- W2076174511 doi "https://doi.org/10.1016/0005-2736(81)90147-4" @default.
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