title: A cyclic nucleotide and calcium-independent protein kinase of chick brain: activation by a heat-stable protein.
abstract: A heat-stable trichloracetic acid-stable protein fraction stimulates protein kinase activity in chick brain cytosol. This protein kinase (tentatively referred to as protein kinase S) can be partially purified by chromatography on DEAE-cellulose and Sepharose G-100. The partially purified protein kinase has an absolute requirement for magnesium and the heat-stable protein for the phosphotransferase activity and is not influenced by cyclic nucleotides, calcium or ethylenediaminetetraacetic acid. The substrate specificity of protein kinase S indicates that it is not a casein kinase and prefers histones over the substrates tested. The specific activity of this protein kinase changes with chick brain development and the activity increased by two-fold by the second post-hatch week, suggesting a role of this protein kinase in chick brain development.
mesh_terms: D000818:Animals; D001923:Brain Chemistry; D002352:Carrier Proteins / Q000502:physiology*; D002417:Cattle; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004789:Enzyme Activation; D047908:Intracellular Signaling Peptides and Proteins; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; D010761:Phosphorus Radioisotopes; C015482:protein kinase modulator; D011494:Protein Kinases