| Autor: |
Gabrielli, Brian, Wettenhall, Richard E.H., Kemp, Bruce E., Quinn, Michael, Bizonova, Lily |
| Zdroj: |
FEBS Letters; January 1984, Vol. 175 Issue: 2 p219-226, 8p |
| Abstrakt: |
A trypsin-activated protein kinase has been isolated from rat liver using a peptide analogue of ribosomal protein S6 as a substrate in kinase assays. The structure of the peptide, Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala, was based on a region of S6 containing both an insulin- and cyclic AMP-regulated phosphorylation site. The trypsin-activated protein kinase phosphorylated a corresponding site in the peptide analogue and ribosomal protein S6 that was distinct from the preferred site for cyclic AMP-dependent protein kinase. Ribosomal S6 contained at least one other major site for the trypsin-activated protein kinase. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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