| Autor: |
Ovchinnikov, Lev P., Motuz, Lyudmila P., Natapov, Pavel G., Averbuch, Lidiya J., Wettenhall, Richard E.H., Szyszka, Ryszard, Kramer, Gisela, Hardesty, Boyd |
| Zdroj: |
FEBS Letters; January 1990, Vol. 275 Issue: 1 p209-212, 4p |
| Abstrakt: |
Elongation factor 2 (EF-2) of rabbit reticulocytes was phosphorylated in vitro by incubation with partially purified EF-2 kinase and (γ 32P)ATP. After exhaustive tryptic hydrolysis 4 phosphopeptides were revealed by two-dimensional peptide mapping. The phosphopeptides were isolated by high performance liquid chromatography and sequenced. A comparison of the primary structure of the phosphopeptides with that of EF-2 showed that all 4 phosphopeptides originated from one region of EF-2 located near the N-terminus that contains 3 threonine residues: Thr-53, Thr-56, Thr-58. A direct estimation of localization of radioactive phosphate in the phosphopeptides demonstrated that all the enumerated threonine residues in EF-2 can be phosphorylated in vitro. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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