Kinetic cooperativity change after H2O2 modification of (Na,K)-ATPase

• Published in: The Journal of biological chemistry Vol. 259; no. 12; pp. 7712 - 7718
• Main Authors: Garner, M H, Garner, W H, Spector, A
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.06.1984; American Society for Biochemistry and Molecular Biology
• Subjects: Adenosine Triphosphate - metabolism; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Cattle; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrogen Peroxide - metabolism; Hydrolases; Hydrolysis; Kidney Medulla - enzymology; Kinetics; Lens, Crystalline - enzymology; Mathematics; Nitrophenols - metabolism; Organophosphorus Compounds - metabolism; Sodium-Potassium-Exchanging ATPase - metabolism; Enzyme; Molecular interaction; Hydrogen Peroxides; Biological activity; Kidney; Vertebrata; Chemical modification; Mammalia; Sodium; Na,K-ATPase; Lens; Artiodactyla; Beef; Kinetics; Catalyst activity; Potassium; Ungulata

The kinetics of hydrolysis of ATP and p-nitrophenylphosphate and the action of the allosteric effectors, Na+ and K+, upon the hydrolysis of these substrates were used to study the H2O2-modified, uncoupled (Na,K)-ATPase isolated from cultured bovine lenses ( Garner , W. H., Garner , M. H., and Specto...