title: The effect of phosphorylation of the EF-2 isolated from rat liver cells on protein biosynthesis in vitro.
abstract: The activity of EF-2 was distinctly decreased after phosphorylation catalysed by a partly purified calmodulin and Ca2+ dependent protein kinase III. At the same time 32P from [gamma-32P]ATP was incorporated into EF-2 molecule. After dephosphorylation of EF-2 catalysed by alkaline phosphatase the activity of this factor was increased. This suggests that the phosphorylation-dephosphorylation of EF-2 is the regulatory process in the elongation step of the translation. Preliminary purification of the kinase III from rat liver resulted in 8-fold purified enzyme with a recovery of 60%.
authors.affiliation: Department of General and Organic Chemistry, Institute of Chemistry, Medical Academy, Białystok, Poland.
authors.forename: A
authors.initials: A
authors.lastname: Gajko
authors.forename: K
authors.initials: K
authors.lastname: Sredzińska
authors.forename: C
authors.initials: C
authors.lastname: Marcinkiewicz
authors.forename: W
authors.initials: W
authors.lastname: Gałasiński
mesh_terms: D000818:Animals; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000096:biosynthesis / Q000378:metabolism*; D010750:Phosphoproteins / Q000096:biosynthesis / Q000378:metabolism*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000302:isolation & purification; D051381:Rats; D012269:Ribosomal Proteins / Q000096:biosynthesis / Q000378:metabolism*
chemical_list: D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D010750:Phosphoproteins; D012269:Ribosomal Proteins; D010770:Phosphotransferases