Interconversion of cyclic nucleotide-activated and cyclic nucleotide-independent forms of a protein kinase from beef heart.

نویسندگان

  • J Erlichman
  • A H Hirsch
  • O M Rosen
چکیده

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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عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 68 4  شماره 

صفحات  -

تاریخ انتشار 1971