Purification and characterisation of adenosine-3',5'-phosphate-independent protein kinase from wheat germ.
cAMP-independent protein kinase was isolated from the wheat germ and purified to electrophoretic homogeneity. The molecular weight of enzyme was approximately 20,000, Km for ATP was (1 +/- 0.2) x 10(-5) M. V was 215 nmol phosphate mg enzyme-1 min-1, and the isoelectric point was at pH 9.2. The enzyme promotes phosphorylation of casein and crude wheat germ ribosomes.
D002845:Chromatography; D000242:Cyclic AMP / Q000494:pharmacology; D006882:Hydroxyapatites; D010944:Plants / Q000201:enzymology*; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D012685:Sepharose; D012995:Solubility; D013379:Substrate Specificity; D014908:Triticum / Q000201:enzymology
D006882:Hydroxyapatites; D012685:Sepharose; D000242:Cyclic AMP; D011494:Protein Kinases