title: Purification and partial characterization of a putative mediator of insulin action on cyclic AMP-dependent protein kinase.
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.
mesh_terms: D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D007295:Inositol Phosphates; D007328:Insulin / Q000378:metabolism*; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000032:analysis; D010455:Peptides / Q000302:isolation & purification*; D011134:Polysaccharides; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D011972:Receptor, Insulin / Q000302:isolation & purification*
chemical_list: D007295:Inositol Phosphates; D007328:Insulin; D009124:Muscle Proteins; D010455:Peptides; D011134:Polysaccharides; D047428:Protein Kinase Inhibitors; C028039:inositol phosphate glycan; D011494:Protein Kinases; D011972:Receptor, Insulin