Comparison of adenosine 3':5'-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle.

@article{Hofmann1975ComparisonOA,
  title={Comparison of adenosine 3':5'-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle.},
  author={Franz Hofmann and Joseph A. Beavo and Peter J Bechtel and Edwin G. Krebs},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 19},
  pages={7795-801}
}
Homogeneous preparations of adenosine 3':5'-monophosphate (cyclic AMP)-dependent protein kinase from rabbit skeletal (Peak I) and bovine heart muscle have been compared. Each enzyme has an S20,w value of 7.0. Each enzyme binds 2 mol of cyclic AMP per mol of enzyme and is dissociated in the presence of saturating concentrations of cyclic AMP into a demeric regulatory subunit-cyclic AMP complex and two catalytic subunits. The isolated subunits recombine, resulting in the formation of the original… CONTINUE READING

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