Reference : Phosphorylation of the Ca2+-pumping ATPase of heart sarcolemma and erythrocyte plasma...
Scientific journals : Article
Human health sciences : Cardiovascular & respiratory systems
http://hdl.handle.net/10993/18083
Phosphorylation of the Ca2+-pumping ATPase of heart sarcolemma and erythrocyte plasma membrane by the cAMP-dependent protein kinase.
English
Neyses, Ludwig mailto [University of Luxembourg > Central Administration >]
Reinlib, L. [> >]
Carafoli, E. [> >]
1985
The Journal of biological chemistry
260
18
10283-7
Yes (verified by ORBilu)
International
0021-9258
UNITED STATES
[en] Animals ; Antigen-Antibody Complex ; Calcium/metabolism ; Calcium-Transporting ATPases/blood/isolation & purification/metabolism ; Cattle ; Erythrocyte Membrane/enzymology ; Immune Sera ; Kinetics ; Molecular Weight ; Myocardium/enzymology ; Phosphorylation ; Protein Kinases/metabolism ; Sarcolemma/enzymology
[en] The Ca2+ ATPase of heart 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.
http://hdl.handle.net/10993/18083
http://www.jbc.org/content/260/18/10283.long

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