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Title: Isolation and properties of cyclic AMP-dependent protein kinase from Dictyostelium discoideum. Author: Schoen C, Arents JC, Van Driel R. Journal: Biochim Biophys Acta; 1984 Jan 18; 784(1):1-8. PubMed ID: 6318830. Abstract: Cyclic AMP-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) in Dictyostelium discoideum was shown to be developmentally controlled. No activity was measured in vegetative cells, but activity increased rapidly during differentiation. A simple procedure for the isolation of the catalytic subunit of the kinase from aggregating cells is presented. The cyclic AMP-dependent holoenzyme could be reconstituted by adding purified D. discoideum cyclic AMP-binding protein. Molecular weight, kinetic parameters, pH dependence and affinity for cyclic AMP were determined for the enzyme. Most properties are similar to those of cyclic AMP-dependent kinase from mammalian cells.[Abstract] [Full Text] [Related] [New Search]