Extracts obtained from rat hepatocytes incubated with saline, glucagon or insulin were electrophoresed on polyacrylamide gels and then assayed for cyclic (3H)AMP binding capacity. Analysis of the binding patterns demonstrated that glucagon dissociated a holoenzyme of cyclic AMP-dependent protein kin
Purification and partial characterization of a putative mediator of insulin action on cyclic AMP-dependent protein kinase
โ Scribed by M. P. Thompson; J. Larner; Daniel L. Kilpatrick
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 607 KB
- Volume
- 62
- Category
- Article
- ISSN
- 0300-8177
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โฆ Synopsis
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.
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