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Plant and Cell Physiology, 1992, Vol. 33, No. 4 407-412
© 1992

Isolation and Characterization of a Cytokinin-Binding Protein from the Water-Soluble Fraction of Tobacco Leaves

Eiki Momotani1 and Hideo Tsuji

Department of Botany, Faculty of Science, Kyoto University Kyoto, 606-01 Japan

Cytokinin-binding protein (CBPI) was purified from the water soluble fraction of tobacco leaves by successive chromatography on benzyladenine-linked (BA-linked) Sepharose 4B, TSK-Gel G3000SWXL, t-zeatin-linked Sepharose 6B and TSK-Gel G3000SWXL. CBPI was obtained as a monomer with a molecular weight of 31 kDa. It has one cytokinin-binding site, which shows a high affinity for BA (Kd=1.1x10–7 M) and other cytokinins. Biologically active cytokinins competed with BA for binding to this protein, while biologically inactive analogues of adenine did not. In all cases, cytokinin-binding activity was assayed by equilibrium dialysis.

1 Present address: National Institute for Basic Biology, Okazaki, 444 Japan.

(Received October 30, 1991; Accepted March 7, 1992)
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