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Plasma membrane calcium pump atpase is not a substrate for cgmp dependent protein kinase

Plasma membrane calcium pump atpase is not a substrate for cgmp dependent protein kinase

Journal of Biochemistry (Tokyo) 111(5): 559-562

A plasma membrane Ca2+-pump ATPase preparation purified from porcine aorta was incubated with cGMP-dependent protein kinase (G-kinase) under the conditions under which dose-dependent stimulation of the enzyme by G-kinase was observed. Several proteins were phosphorylated, but two isoforms of plasma membrane Ca2-pump ATPase with molecular masses of 135- and 145-kDa were not phosphorylated. The protein that was phosphorylated by G-kinase and identified in our previous study as the 135-kDa isoform of Ca2+-pump ATPase on the basis of its almost identical mobility on SDS-PAGE, was found to be another protein with a molecular mass of 138 kDa. Fractionation of the enzyme preparation after incubation with G-kinase by a newly developed calmodulin affinity chromatographic method resulted in the separation of all the G-kinase substrates from the two isoforms of plasma membrane Ca2+-pump ATPase. These results suggest that the direct phosphorylation of the Ca2+-pump ATPase does not occur in association with the stimulation of plasma membrane Ca2+-pump ATPase by G-kinase.

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