title: Cyclic AMP-dependent and independent protein kinases in Ascaridia galli.
abstract: The occurrence of multiple protein kinases, distinguished with respect to molecular weight and preference for acceptor proteins, was demonstrated in Ascaridia galli. The molecular weights of the cyclic AMP-dependent protein kinase and of phosvitin kinase I and II - both independent of cyclic AMP-were determined to be 160000, greater than 200000 and 40000, respectively. The cyclic AMP-dependent protein kinase preferred histones and kemptide as acceptor substrates; stimulation of enzyme activity was up to 4-fold by cyclic AMP. The activities of phosvitin kinase I and II were found to be effectively inhibited by suramin. The inhibition constants were calculated to be 2 microM and 5 microM, respectively. In addition, stibophen turned out to be a potent inhibitor of phosvitin kinase I; the inhibition constant was determined to be 10 microM.
mesh_terms: D000818:Animals; D001197:Ascaridia / Q000201:enzymology*; D001557:Benzenesulfonates / Q000494:pharmacology; D000242:Cyclic AMP / Q000502:physiology; D010774:Phosvitin / Q000378:metabolism; D006656:Protamine Kinase / Q000378:metabolism; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D013498:Suramin / Q000494:pharmacology
chemical_list: D001557:Benzenesulfonates; D047428:Protein Kinase Inhibitors; D013498:Suramin; D010774:Phosvitin; D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase