Purification and partial characterization of two cyclic amp-independent protein kinases from AH-66 hepatoma cells.
Two cyclic AMP-independent protein kinases (CK 1 and CK 2) in the cytosol fraction of AH-66 hepatoma cells have been purified to homogeneity. CK 1 and CK 2 had molecular weights of 36,000 and 340,000, respectively, as determined by gel filtration. CK 1 consists of a single polypeptide and CK 2 is composed of two subunits of 42,000 and 26,000 molecular weights. CK 1 and the 26,000 molecular weight subunit of CK 2 were autophosphorylated. Both enzymes catalyzed the phosphorylation of cytosolic proteins including those with molecular weights of 125,000, 95,000, 56,000, and 40,000.
D000818:Animals; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D000242:Cyclic AMP / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000145:classification / Q000302:isolation & purification*; D051381:Rats; D013379:Substrate Specificity
D000242:Cyclic AMP; D011494:Protein Kinases