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Purification and partial characterization of a putative mediator of insulin action on cyclic AMP-dependent protein kinase

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Summary

An insulin mediator which inhibits cAMP-dependent protein kinase has been purified approximately 1 000 2 000-fold from skeletal muscle. Following heat treatment, charcoal adsorption and Sephadex G-25 sieving, Sephadex G-15 sieving and HPLC over an anion exchange column were performed. The mediator has characteristics of a relatively low molecular weight peptide or derivatized peptide which acts on cAMP-dependent protein kinase but not on mitochondrial pyruvate dehydrogenase.

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Thompson, M.P., Larner, J. & Kilpatrick, D.L. Purification and partial characterization of a putative mediator of insulin action on cyclic AMP-dependent protein kinase. Mol Cell Biochem 62, 67–75 (1984). https://doi.org/10.1007/BF00230079

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Keywords

  • Peptide
  • Protein Kinase
  • Pyruvate
  • Charcoal
  • Heat Treatment