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Phosphorylation of fodrin (nonerythroid spectrin) by the purified insulin receptor kinase

✍ Scribed by Takashi Kadowaki; Eisuke Nishida; Masato Kasuga; Tetsu Akiyama; Fumimaro Takaku; Masaharu Ishikawa; Hikoichi Sakai; Satish Kathuria; Yoko Fujita-Yamaguchi


Book ID
117056805
Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
1000 KB
Volume
127
Category
Article
ISSN
0006-291X

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πŸ“œ SIMILAR VOLUMES


Phosphorylation of the insulin receptor
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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

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✍ Elizabeth M. Sale; Morris F. White; C. Ronald Kahn πŸ“‚ Article πŸ“… 1987 πŸ› John Wiley and Sons 🌐 English βš– 708 KB

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