doi: 10.1111/j.1432-1033.1980.tb04613.x.
Purification and characterisation of adenosine-3',5'-phosphate-independent protein kinase from wheat germ
- PMID: 6249581
- DOI: 10.1111/j.1432-1033.1980.tb04613.x
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Purification and characterisation of adenosine-3',5'-phosphate-independent protein kinase from wheat germ
Eur J Biochem.
1980 May.
Free article
Abstract
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.
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