Purification and characterisation of adenosine-3',5'-phosphate-independent protein kinase from wheat germ |
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Authors: | W Rychlik W Zagórski |
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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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