Dissociation of the hepatic insulin receptor favours its phosphorylation by casein kinase 2
β Scribed by Ramon Trujillo; Marta Jose; Maria Plana; Elena Molina; Emilio Itarte
- Book ID
- 115924856
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 643 KB
- Volume
- 283
- Category
- Article
- ISSN
- 0014-5793
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Insulin receptor was examined as a substrate for the multipotential protein kinase casein kinase I. Casein kinase I phosphorylated partially purified insulin receptor from human placenta as shown by immunoprecipitation of the complex with antiserum to the insulin receptor. Analysis of the phosphoryl
Various glycolytic and gluconeogenic enzymes were tested as substrates for the insulin receptor kinase. Phosphofructokinase and phosphoglycerate mutase were found to be the best substrates. Phosphorylation of these enzymes was rapid, stimulated 2-to 6-fold by M insulin and occurred exclusively on ty