The K+-dependent phosphatase from human renal tissue: its properties and time dependent inhibition by ouabain.
The K+-dependent p-nitrophenyl phosphatase activity associated with human renal (Na+ + K+)-ATPase was examined for some of its kinetic properties. ATP inhibited the K+-dependent phosphatase and raised the Km for p-nitrophenylphosphate. Stimulation of the K+-dependent phosphatase by K+ was blocked by Na+ in a noncompetitive manner. Inhibition of the K+-dependent phosphatase by ouabain was dependent upon incubation time. The apparent Kï was 2.0 micron.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology*; D010042:Ouabain / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011188:Potassium / Q000378:metabolism / Q000494:pharmacology; D012964:Sodium / Q000378:metabolism / Q000494:pharmacology; D013997:Time Factors
D010042:Ouabain; D000255:Adenosine Triphosphate; D012964:Sodium; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D011188:Potassium