Adenosine 3',5'-monophosphate-dependent protein kinase of cultured mammalian cells.
Protein kinase was partially purified from Chang's liver cells, 3T6 mouse embryo fibroblasts, and HeLa cells. The rate of histone phosphorylation catalyzed by the kinase from each of these cell lines was stimulated two- to three-fold by 1 x 10(-6) molar adenosine 3',5'-monophosphate. The same concentration of guanosine 3',5'-monophosphate failed to stimulate these kinases.
D000227:Adenine Nucleotides; D002460:Cell Line; D046508:Culture Techniques; D000242:Cyclic AMP; D005347:Fibroblasts / Q000201:enzymology; D006367:HeLa Cells / Q000201:enzymology; D006657:Histones / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D010770:Phosphotransferases / Q000302:isolation & purification*
D000227:Adenine Nucleotides; D006657:Histones; D000242:Cyclic AMP; D010770:Phosphotransferases