
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.
Reticulocytes, Gossypol, Chromatography, Ion Exchange, Peptide Elongation Factors, Staurosporine, Guanosine Diphosphate, Chromatography, Affinity, Histones, Molecular Weight, Kinetics, Alkaloids, Peptide Elongation Factor 1, Animals, Electrophoresis, Polyacrylamide Gel, Rabbits, Phosphorylation, Ribosomes, Protein Kinase C
Reticulocytes, Gossypol, Chromatography, Ion Exchange, Peptide Elongation Factors, Staurosporine, Guanosine Diphosphate, Chromatography, Affinity, Histones, Molecular Weight, Kinetics, Alkaloids, Peptide Elongation Factor 1, Animals, Electrophoresis, Polyacrylamide Gel, Rabbits, Phosphorylation, Ribosomes, Protein Kinase C
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