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  • Title: ATPase and phosphatase activities from human red cell membranes. III. Stimulation of K+-activated phosphatase by phospholipase C.
    Author: Richards DE, Garrahan PJ, Rega AF.
    Journal: J Membr Biol; 1977 Jun 30; 35(2):137-47. PubMed ID: 142159.
    Abstract:
    Treatment of red cell membranes with pure phospholipase C inactivates (Na+ + K+)-ATPase activity and Na+-dependent phosphorylation but increases K+-dependent phosphatase activity. When phospholipase A2 replaces phospholipase C, all activities are lost. Activation of K+-dependent phosphatase by treatment with phospholipase C is caused by an increase in the maximum rate of hydrolysis of p-nitrophenylphosphate and in the maximum activating effect of K+, the apparent affinities for substrate and cofactors being little affected. After phospholipase C treatment K+-dependent phosphatase is no longer sensitive to ouabain but becomes more sensitive to N-ethylmaleimide. In treated membranes Na+ partially replaces K+ as an activator of the phosphatase. Although ATP still inhibits phosphatase activity, neither ATP, nor ATP+Na+ are able to modify the apparent affinity for K+ of K+-dependent phosphatase in these membranes.
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