Inhibitory characteristics of indomethacin on the activation of K+-dependent p-nitrophenylphosphatase by both Na+ and ATP in vitro.
1. The activation of K+-NPPase by both Na+ and ATP was inhibited by indomethacin in vitro. 2. Indomethacin concentration required for 50% inhibition was 6.25 X 10(-4) M. 3. Inhibition manners of indomethacin for Na+ and ATP were competitive type and noncompetitive type, respectively. 4. The Ki values for indomethacin for Na+ and ATP were 1.4 X 10(-4) M and 8.8 X 10(-4) M, respectively. 5. The inhibitory effect of indomethacin was reversible.
D009597:4-Nitrophenylphosphatase / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D001667:Binding, Competitive; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D007213:Indomethacin / Q000494:pharmacology*; D007700:Kinetics; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011188:Potassium / Q000502:physiology*; D012964:Sodium / Q000494:pharmacology*; D013552:Swine; D013997:Time Factors
D000255:Adenosine Triphosphate; D012964:Sodium; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D011188:Potassium; D007213:Indomethacin