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Cyclic AMP Stimulation of Membrane Phosphorylation and Ca(2+)-Activated, Mg(2+)-Dependent ATPase in Cardiac Sarcoplasmic Reticulum.

机译:环磷酸腺苷对心肌肌浆网中膜磷酸化和Ca(2 +)激活的mg(2+)依赖性aTp酶的刺激作用。

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摘要

Ca(2+)-activated ATPase (EC3.6.1.15) in canine cardiac sarcoplasmic reticulum was stimulated 50-80% by cyclic adenosine 3' :5'-monophosphate. The relationship of this stimulation to cyclic AMP-dependent membrane phosphorylation with phosphoester bands was studied. Cyclic AMP stimulation of ATPase activity was specific for Ca(2+)-activated ATPase and was half-maximal at about 0.1 micrometers which is similar to the concentration required for half-maximal stimulation of membrane phosphorylation by endogenous cyclic AMP-stimulated protein kinase (EC 2.7.1.37). Cyclic AMP stimulation of Ca(2+)-activated ATPase was calcium dependent and maximal at calculated Ca(2+) concentrations of 2.0 micrometers. Cyclic AMP-dependent CA(2+)-activated ATPase correlated well with the cyclic AMP-dependent membrane phosphorylation of which 80% was 20,000 molecular weight protein identified by sodium dodecyl sulfate discontinuous polyacrylamide gel electrophoresis.

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