Phosphorylation of the porcine skeletal and cardiac muscle sarcoplasmic reticulum ryanodine receptor.

@article{Strand1993PhosphorylationOT,
  title={Phosphorylation of the porcine skeletal and cardiac muscle sarcoplasmic reticulum ryanodine receptor.},
  author={M A Strand and Charles Francis Louis and James R. Mickelson},
  journal={Biochimica et biophysica acta},
  year={1993},
  volume={1175 3},
  pages={319-26}
}
Porcine skeletal and cardiac muscle sarcoplasmic reticulum (SR) vesicle fractions enriched in the ryanodine receptor were phosphorylated in the presence of [gamma-32P]MgATP and either exogenous cAMP-dependent protein kinase (cAMP-PK), or Ca2+ plus calmodulin. Phosphorylation of the cardiac muscle ryanodine receptor in the presence of either cAMP-PK or calmodulin (6.4 and 10.6 pmol Pi/mg SR respectively) was approximately equal to or twice the [3H]ryanodine binding activity of this preparation… CONTINUE READING
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