| Autor: |
Diggle, T A, Schmitz-Peiffer, C, Borthwick, A C, Welsh, G I, Denton, R M |
| Zdroj: |
Biochemical Journal; October 1991, Vol. 279 Issue: 2 p545-551, 7p |
| Abstrakt: |
Casein kinase 2 activity as measured by phosphorylation of the peptide substrate Arg-Arg-Arg-Glu-Glu-Glu-Thr-Glu-Glu-Glu is increased by about 50% in extracts from insulin-treated epididymal fat-pads or isolated fat-cells after purification by Mono Q chromatography. Insulin acts to increase the Vmax. of the kinase. An acid-soluble protein with an apparent subunit molecular mass of about 22 kDa appears to be a substrate for casein kinase 2. The protein possesses a number of properties in common with the acid-soluble heat-stable 22 kDa protein which exhibits increased phosphorylation in rat adipose tissue exposed to insulin. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
