Purification and partial characterization of a putative mediator of insulin action on cyclic AMP-dependent protein kinase |
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| Authors: | M. P. Thompson J. Larner Daniel L. Kilpatrick |
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| Affiliation: | (1) Department of Pharmacology, University of Virginia Medical School, 22903 Charlottesville, VA, U.S.A.;(2) Roche Institute of Molecular Biology, 07110 Nutley, NJ, U.S.A.;(3) Present address: Department of Biochemistry, University of Otago, Box 56, Dunedin, New Zealand |
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| Abstract: | 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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