Abstract
Glucagon and insulin both stimulated the 32P-labelling of ribosomal protein S6 in rat hepatocytes that had been incubated with 32Pi. Glucagon selectively enhanced the labelling of the tryptic peptide phosphorylated by cyclic AMP-dependent protein kinase, demonstrating that 6 S is a physiological substrate for this enzyme. Insulin stimulated the phosphorylation of distinct tryptic peptides, at least one of which appears to be very close in the primary structure to the sites phosphorylated by cyclic AMP-dependent protein kinase.
Original language | English |
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Pages (from-to) | 207-213 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 148 |
Issue number | 2 |
DOIs | |
Publication status | Published - 8 Nov 1982 |
Keywords
- Cyclic AMP
- Glucagon
- Hepatocytes
- Insulin
- Protein synthesis
- Ribosomes
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology