PMID: 39261Jun 18, 1979

The effect of vanadate on human kidney potassium dependent phosphatase

Naunyn-Schmiedeberg's Archives of Pharmacology
G L NiederP A Culp


This study examined the effects of vanadate on the potassium dependent phosphatase activity present in purified human kidney microsomal (Na+ + K+)-adenosine triphosphatase. Vanadate anion inhibited the K+-dependent phosphatase at a K1 of 35 nM. This inhibition was noncompetitive with the substrate, p-nitrophenylphosphate. The inhibition by vanadate at 1 mM K+ was only 45% of the inhibition that was observed at 10 mM K+. Neither preincubation of the enzyme with vanadate, nor changing the pH of the assay from 8.2 to 7.2 had any effect on the K1 for vanadate. The inclusion of 2.5 mM isoproterenol, to complex the yanadate, reversed the inhibition, as did diluting the enzymatic reaction. Vanadate also inhibited the overall (Na+ + K+)-ATPase reaction at a K1 of 1.91 microM. This inhibition was also reversible upon inclusion of isoproterenol in the assay. Increasing the level of magnesium from 6 mM to 30 mM lowered the K1 of vanadate to 0.25 microM. The possible role of vanadate as a physiological mediator of (Na+ + k+)-atpase activity is discussed.


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Jun 16, 1981·Biochemical and Biophysical Research Communications·F VyskocilH Dlouhá


Apr 12, 1977·Biochimica Et Biophysica Acta·J M Braughler, C N Corder
Jul 1, 1975·Journal of Applied Physiology·A N CharneyF H Epstein
Nov 30, 1976·Biochemistry·L C Cantley, L Josephson
Aug 8, 1977·Biochemical and Biophysical Research Communications·P M Hudgins, G H Bond
Oct 18, 1977·Biochemistry·L Josephson, L C Cantley
Sep 7, 1978·Nature·I HackbarthG Philipp
Jul 1, 1978·The Science of the Total Environment·A R Byrne, L Kosta
Oct 26, 1978·Nature·W E BalfourI M Glynn
Dec 1, 1965·Proceedings of the Society for Experimental Biology and Medicine·R J Rifkin

Related Concepts

Phosphoric Monoester Hydrolases
Magnesium Measurement
Adenosine Triphosphatases
Phosphoric Monoester Hydrolase Activity
Mediator of activation protein

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