Mechanism of activation by adenosine 3':5'-cyclic monophosphate of a protein phosphokinase from rabbit reticulocytes.

@article{Tao1970MechanismOA,
  title={Mechanism of activation by adenosine 3':5'-cyclic monophosphate of a protein phosphokinase from rabbit reticulocytes.},
  author={Mariano Tao and Maria Luisa Salas and Fritz Albert Lipmann},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1970},
  volume={67 1},
  pages={
          408-14
        }
}
  • M. TaoM. SalasF. Lipmann
  • Published 1 September 1970
  • Biology, Chemistry
  • Proceedings of the National Academy of Sciences of the United States of America
Two protein phosphokinases (EC 2.7.1.37) were found to be present in rabbit reticulocytes. The two enzymes were separated by DEAE-cellulose chromatography and called kinases I and II. Adenosien 3':5'-cyclic monophosphate stimulated the activity of both enzymes. However, the degree of stimulation was different and depended on the protein acceptor used. In the presence of adenosine 3':5'-cyclic monophosphate, protein kinase I dissociated into two subunits: a subunit binding adenosine 3':5'-cyclic… 
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MECHANISM OF ACTIVATION OF A RABBIT RETICULOCYTE PROTEIN KINASE BY ADENOSINE 3′,5′‐CYCLIC MONOPHOSPHATE *

  • M. Tao
  • Biology
    Annals of the New York Academy of Sciences
  • 1971
Experimental evidence will be presented to suggest a possible mode of action of the cyclic nucleotide on some of these enzymes, particularly kinase I, which has been found to have a strong affinity for cyclic AMP.

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