Staurosporine and gossypol are inhibitors of the function of peptide elongation factor 1 alpha from rabbit reticulocytes
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články
PubMed
8032322
Knihovny.cz E-zdroje
- MeSH
- alkaloidy farmakologie MeSH
- chromatografie afinitní MeSH
- chromatografie iontoměničová MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- elongační faktor 1 MeSH
- elongační faktory antagonisté a inhibitory krev izolace a purifikace MeSH
- fosforylace MeSH
- gossypol farmakologie MeSH
- guanosindifosfát farmakologie MeSH
- histony metabolismus MeSH
- kinetika MeSH
- králíci MeSH
- molekulová hmotnost MeSH
- proteinkinasa C antagonisté a inhibitory MeSH
- retikulocyty metabolismus MeSH
- ribozomy metabolismus MeSH
- staurosporin MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- alkaloidy MeSH
- elongační faktor 1 MeSH
- elongační faktory MeSH
- gossypol MeSH
- guanosindifosfát MeSH
- histony MeSH
- proteinkinasa C MeSH
- staurosporin 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.
