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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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Author notes

  1. M. P. Thompson

    Present address: Department of Biochemistry, University of Otago, Box 56, Dunedin, New Zealand

Authors and Affiliations

  1. Department of Pharmacology, University of Virginia Medical School, 22903, Charlottesville, VA, U.S.A.

    M. P. Thompson & J. Larner

  2. Roche Institute of Molecular Biology, 07110, Nutley, NJ, U.S.A.

    Daniel L. Kilpatrick

Authors
  1. M. P. Thompson
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  2. J. Larner
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  3. Daniel L. Kilpatrick
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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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  • DOI: https://doi.org/10.1007/BF00230079

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