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Isolation and properties of cyclic AMP-dependent protein kinase from Dictyostelium discoideum.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 1984 Jan 18; Vol. 784 (1), pp. 1-8. - Publication Year :
- 1984
-
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.
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 784
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 6318830
- Full Text :
- https://doi.org/10.1016/0167-4838(84)90165-1