title: Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells.
abstract: The elongation factor 2 (eEF-2) protein kinase was isolated from rat liver cells, purified and partly characterized. It was found that the enzyme exists in an inactive form in the homogenate of rat liver. The active fraction of kinase eEF-2 was obtained after removal of the inhibitory substance by hydroxyapatite column chromatography. The purified enzyme is an electrophoretically homogeneous protein with relative molecular mass of approximately 90,000 and isoelectric point, pI = 5.9. The enzyme specifically phosphorylates the elongation factor eEF-2 in the presence of calmodulin and Ca2+.
authors.affiliation: Department of General and Organic Chemistry, Medical Academy, Białystok, Poland.
authors.forename: A
authors.initials: A
authors.lastname: Gajko
authors.forename: W
authors.initials: W
authors.lastname: Gałasiński
authors.forename: A
authors.initials: A
authors.lastname: Gindzieński
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism; D054736:Elongation Factor 2 Kinase; D008099:Liver / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D051381:Rats; D017208:Rats, Wistar; D013379:Substrate Specificity
chemical_list: D002147:Calmodulin; C517691:Eef2k protein, rat; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D054736:Elongation Factor 2 Kinase; D002118:Calcium