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Purification and partial characterization of a putative mediator of insulin action on cyclic AMP-dependent protein
Molecular and Cellular Biochemistry
|April 1, 1984
Abstract:
An insulin mediator which inhibits cAMP-dependent protein kinase has been purified approximately 1000-2000-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.