Characterization of protein kinases from Blepharisma intermedium.
Three protein kinases (EC 2.7.1.37) were detected in Blepharisma and partially purified. The enzymes were most active with histone as substrate protein. The stability of the bond between phosphate and protein acceptor showed the characteristics of seryl- or threonylphosphate. Protein kinase I was solubilized by ultrasonication or freezing and thawing, while the enzymes II and III were readily solubilized by mild homogenization. Protein II and III were noticeably activated by cAMP and cGMP, while protein kinase I was inhibited by cAMP. Associated with protein kinase II and III activity was the ability to bind labeled cAMP. The following molecular weights were determined: 90000 for enzyme I, 280000 for enzyme II, and 95000 for enzyme III. Various apparent Michaelis constants were estimated.
D016798:Ciliophora / Q000201:enzymology*; D000242:Cyclic AMP / Q000378:metabolism; D004355:Drug Stability; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D006656:Protamine Kinase; D011494:Protein Kinases / Q000302:isolation & purification; D013347:Subcellular Fractions / Q000201:enzymology; D013696:Temperature
D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase