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Phosphorylation of the calcium pumping atpase of heart sarcolemma and erythrocyte plasma membrane by the cyclic amp dependent protein kinase

Phosphorylation of the calcium pumping atpase of heart sarcolemma and erythrocyte plasma membrane by the cyclic amp dependent protein kinase

Journal of Biological Chemistry 260(18): 10283-10287

ISSN/ISBN: 0021-9258

The Ca2+-ATPase of heart [beef] sarcolemma was stimulated by the exposure of sarcolemma vesicles to ATP and the catalytic subunit of the cAMP-dependent protein kinase. The effect of the phosphorylation system was primarily on the Km (Ca2+) of the pumping ATPase. The ATPase purified from heart sarcolemma or erythrocytes became phosphorylated under the conditions mentioned above. Hydroxylamine treatment of the labeled ATPase has shown that the phosphorylation was additive to be acylphosphate formed on the ATPase during the reaction cycle. The stoichiometry of the kinase-promoted phosphorylation (i.e. the fraction of the ATPase molecules that became labeled) approached 30% with both the heart and the erythrocyte enzyme.

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Accession: 006107905

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Related references

Phosphorylation of the Ca2+-pumping ATPase of heart sarcolemma and erythrocyte plasma membrane by the cAMP-dependent protein kinase. Journal of Biological Chemistry 260(18): 10283-10287, 1985

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