Plant Physiol.
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Plant Physiology 71:482-488 (1983)
© 1983 American Society of Plant Biologists

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Resolution and Properties of a Protein Kinase Catalyzing the Phosphorylation of a Wheat Germ Cytokinin-Binding Protein 1

Gideon M. Polya and Jeffrey R. Davies

Department of Biochemistry, La Trobe University, Bundoora, Victoria 3083 Australia

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. The major polypeptides present in the purified CBP preparations have molecular weights of 60,000 ± 4,000, 42,000 ± 3,000, and 37,000 ± 3,000, respectively. A protein kinase that catalyzes the phosphorylation of CBP (CBP kinase) was extensively purified from wheat germ by affinity chromatography on casein-Sepharose 4B and CBP-Sepharose 4B. The purification procedure resolves CBP kinase from an abundant casein kinase that does not phosphorylate CBP. CBP kinase catalyzes the phosphorylation of casein, phosvitin, CBP, and the wheat germ cyclic AMP-binding protein cABPII. CBP kinase phosphorylates the major 60,000 dalton subunit of CBP as well as 16,000 to 18,000 dalton polypeptides present in CBP preparations. CBP fractions with differing activities as substrates for CBP kinase were partly resolved by gel filtration and by chromatography on DEAE-Sephacel.

1 Supported by a grant from the Australian Research Grants Committee.




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K. VELUTHAMBI and B. W. POOVAIAH
Calcium-Promoted Protein Phosphorylation in Plants
Science, January 13, 1984; 223(4632): 167 - 169.
[Abstract] [PDF]


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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1983 by the American Society of Plant Biologists