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. 1971 Apr;68(4):731–735. doi: 10.1073/pnas.68.4.731

Interconversion of Cyclic Nucleotide-Activated and Cyclic Nucleotide-Independent Forms of a Protein Kinase from Beef Heart

Jack Erlichman 1,2, Allen H Hirsch 1,2, Ora M Rosen 1,2,*
PMCID: PMC389030  PMID: 4323785

Abstract

A protein kinase activated by cyclic nucleotides was purified from beef heart. Upon exposure to adenosine 3′:5′-cyclic monophosphate (cyclic AMP) during gel filtration on Sephadex G-200, the protein kinase dissociated into a cyclic nucleotide-independent protein kinase and a cyclic nucleotide-binding protein. A similar or identical cyclic nucleotide-independent protein kinase could be obtained in highly purified form by clution from a DEAE-cellulose column with 10-6 M cyclic AMP; the cyclic AMP-binding protein was apparently retained by the resin. The addition of cyclic nucleotide-binding protein to cyclic nucleotide-independent protein kinase resulted in the reappearance of cyclic nucleotide-dependent protein kinase, which could be isolated by filtration on Sephadex G-200 in the absence of cyclic AMP. These results confirm and extend previous suggestions that cyclic nucleotides activate protein kinases by dissociating them from inhibitory, cyclic nucleotide-binding proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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