Studies on adenosine 3',5'-phosphate-binding and adenosine 3',5-phosphate-dependent protein kinase activities associated with subcellular fractions of Chinese hamster ovary cells.
Both cyclic AMP-binding and cyclic AMP-dependent protein kinase activities exist in Chinese hamster ovary cell extract. Competition experiments demonstrate that the binding is specific for cyclic AMP. All cellular elements including nucleus, mitochondria, plasma membrane, microsome, ribosome and cytosol contain both activities. Binding activity is highest in the cytosol and lowest in the nucleus. Each fraction contains endogenous protein kinase activity which is insensitive to cyclic AMP activation. When histone was used as a substrate, protein kinase activity in all fractions was stimulated by cyclic AMP (with the highest in cytosol and lowest in the nucleus) and inhibited by Walsh's protein kinase inhibitor.
D000227:Adenine Nucleotides / Q000494:pharmacology; D000818:Animals; D002999:Clone Cells; D006224:Cricetinae; D000242:Cyclic AMP / Q000378:metabolism*; D006152:Cyclic GMP / Q000494:pharmacology; D005260:Female; D006657:Histones / Q000378:metabolism; D010053:Ovary / Q000378:metabolism; D010774:Phosvitin / Q000494:pharmacology; D011485:Protein Binding; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism
D000227:Adenine Nucleotides; D006657:Histones; D047428:Protein Kinase Inhibitors; D010774:Phosvitin; D000242:Cyclic AMP; D011494:Protein Kinases; D006152:Cyclic GMP