Resolution and Properties of a Protein Kinase Catalyzing the Phosphorylation of a Wheat Germ Cytokinin-Binding Protein
作者： Gideon M. Polya , Jeffrey R. Davies
DOI: 10.1104/PP.71.3.482
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摘要: The major cytokinin binding protein of wheat germ (CBP) was extensively purified employing chromatography on Cibacron F3GA-Sepharose CL6B and concanavalin A-agarose as key purification steps. polypeptides present in the CBP preparations have molecular weights 60,000 ± 4,000, 42,000 3,000, 37,000 respectively. A kinase that catalyzes phosphorylation (CBP kinase) from by affinity casein-Sepharose 4B CBP-Sepharose 4B. procedure resolves an abundant casein does not phosphorylate CBP. casein, phosvitin, CBP, cyclic AMP-binding cABPII. phosphorylates dalton subunit well 16,000 to 18,000 preparations. fractions with differing activities substrates for were partly resolved gel filtration DEAE-Sephacel.
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