Effect of temperature on phosphorylation and ouabain binding to N-ethylmaleimide-treated (Na+, K+)-ATPase.

Treatment of purified sodium and potassium ion-activated adenosine triphosphatase from sheep kidney with N-ethylmaleimide in the presence of KC1 and ATP reduced hydrolytic activity by 83% while steady state phosphorylation was inhibited only 24%. At 3O”C, in the presence of magnesium plus inorganic phosphate, the ouabain-binding capacity of the N… CONTINUE READING