Partial purification of a ribonucleic acid cAMP-independent protein kinase from embryonic chicken muscle.
A cAMP-indepedent protein kinase (P38 kinase) from embryonic chicken muscle with ability to phosphorylate a 38,000 molecular weight polypeptide and to bind to RNAs has been further characterized. An approximately 2000-fold purification of this enzyme was achieved by a combination of affinity and ion-exchange chromatography. Our studies indicate that this protein kinase can not phosphorylate the small subunit of rabbit reticulocyte initiation factor eIF-2 in the presence of its normal endogenous substrate, nor is it activated over a wide range of concentrations of double-stranded RNA. This P38 kinase is, therefore, distinct from the hemin-regulated translational inhibitor of protein synthesis in rabbit reticulocytes and from the interferon-induced protein kinase identified In several systems.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002642:Chick Embryo; D002845:Chromatography / Q000379:methods; D000242:Cyclic AMP; D004591:Electrophoresis, Polyacrylamide Gel; D015852:Eukaryotic Initiation Factor-2; D009132:Muscles / Q000201:enzymology*; D010448:Peptide Initiation Factors / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins
D002352:Carrier Proteins; D015852:Eukaryotic Initiation Factor-2; D010448:Peptide Initiation Factors; D011506:Proteins; D016601:RNA-Binding Proteins; D012313:RNA; D000242:Cyclic AMP; D011494:Protein Kinases