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• W1570489146 abstract "Electroplax microsomes enriched in sodium-potassium-activated adenosine triphosphatase are found to catalyze sodium-stimulated, potassium-inhibited hydrolysis of UTP. The microsomes are phosphorylated by [γ-32P]UTP in a (Mg2+ + Na+)-stimulated reaction to yield an acid-stable phosphoprotein. Stimulation of the phosphorylation by Na+ in the presence of Mg2+ is paralleled by stimulation of UTP hydrolysis. K+ inhibits both the Na+-stimulated phosphorylation and hydrolysis in parallel at 0°. UTP and Na+ each partially antagonize the K+ inhibition. The phosphoprotein upon partial proteolysis yields labeled phosphopeptides which have the same electrophoretic mobilities as similarly obtained phosphopeptides after phosphorylation by [γ-32P]ATP. ATP inhibits the UTP phosphorylation and hydrolytic reactions, whereas UTP inhibits the Na+-stimulated and (Na+ + K+)-stimulated ATP hydrolysis. However, the enzyme affinity for UTP is at least 1000 times less than for ATP. Ouabain abolishes the Na+-dependent UTP phosphorylation and hydrolysis, whereas 2,3-dimercaptopropanol-arsenite inhibits only the hydrolysis, which is similar to its action with ATP as substrate. It is concluded that the UTP phosphorylation site is identical with that reactive with ATP and that the same phosphopeptide is involved in the Na+-stimulated hydrolysis of UTP or ATP and the (Na+ + K+)-stimulated hydrolysis of ATP. K+ inhibition of UTP hydrolysis results from inhibition of phosphorylation. Thus, K+ can have at least two separate effects on the enzyme: inhibition of phosphorylation, in addition to the well known activation of dephosphorylation in the presence of ATP. Both of these effects can be explained by a model in which it is assumed that potassium-enzyme has a reduced affinity for nucleotides and Na+. These, on the other hand, reduce the affinity of dephosphoenzyme for K+. In this view, ATP, by virtue of its greater affinity than UTP for the enzyme, is able to reduce the K+ inhibition of phosphorylation, thus permitting the subsequent K+ activation of enzyme dephosphorylation to follow in cycle." @default.
• W1570489146 created "2016-06-24" @default.
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• W1570489146 date "1972-06-01" @default.
• W1570489146 modified "2023-09-26" @default.
• W1570489146 title "Sodium-Potassium-activated Adenosine Triphosphatase: Potassium Regulation of Enzyme Phosphorylation" @default.
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• W1570489146 doi "https://doi.org/10.1016/s0021-9258(19)45187-9" @default.
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