Initiation factor 2 isolated from rat brain contains kinase activities responsible for its phosphorylation.
Initiation factor 2 from adult rat brain was isolated from salt-washed microsomes using a three-step purification process consisting of heparin-Sepharose, phosphocellulose and diethylaminoethyl-cellulose (DEAE cellulose) column chromatographies. The initiation factor 2(eIF-2) was phosphorylated in subunits alpha and beta by the endogenous protein kinase activity present in the pruified preparation. This protein kinase activity proved to be mostly a casein kinase, although the possible presence of a very specific alpha kinase activity cannot be dismissed.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D001923:Brain Chemistry; D002364:Caseins / Q000378:metabolism; D002384:Catalysis; D015852:Eukaryotic Initiation Factor-2; D006657:Histones / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D002364:Caseins; D015852:Eukaryotic Initiation Factor-2; D006657:Histones; D010448:Peptide Initiation Factors; D011506:Proteins; D011494:Protein Kinases