Staurosporine and gossypol are inhibitors of the function of peptide elongation factor 1 alpha from rabbit reticulocytes
Language English Country England, Great Britain Media print
Document type Journal Article
PubMed
8032322
Knihovny.cz E-resources
- MeSH
- Alkaloids pharmacology MeSH
- Chromatography, Affinity MeSH
- Chromatography, Ion Exchange MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Peptide Elongation Factor 1 MeSH
- Peptide Elongation Factors antagonists & inhibitors blood isolation & purification MeSH
- Phosphorylation MeSH
- Gossypol pharmacology MeSH
- Guanosine Diphosphate pharmacology MeSH
- Histones metabolism MeSH
- Kinetics MeSH
- Rabbits MeSH
- Molecular Weight MeSH
- Protein Kinase C antagonists & inhibitors MeSH
- Reticulocytes metabolism MeSH
- Ribosomes metabolism MeSH
- Staurosporine MeSH
- Animals MeSH
- Check Tag
- Rabbits MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Alkaloids MeSH
- Peptide Elongation Factor 1 MeSH
- Peptide Elongation Factors MeSH
- Gossypol MeSH
- Guanosine Diphosphate MeSH
- Histones MeSH
- Protein Kinase C MeSH
- Staurosporine MeSH
As it has been found, the incubation of [gamma-32P]ATP with elongation factor--1 alpha purified from rabbit reticulocytes resulted in the phosphorylation of several substrate proteins /Tuhácková, Z. (1992) In: Rec. Adv. Cell. Mol. Biol. 4, 79-86, Peeters Press, Leuven/ (1). In the present paper chromatofocusing of the purified eEF-1 alpha demonstrates that the ATP-dependent protein kinase activity is associated with a single protein catalyzing the GTP-dependent binding of aminoacyl-tRNA to ribosomes. Both of these activities are inhibited by staurosporine and gossypol. The inhibition by GDP but not by GTP indicates a possible involvement of conformation changes also in the modulation of the protein kinase activity displayed by eEF-1 alpha.
