Purification and Properties of Cytokinin-Binding Proteins from Tobacco Leaves |
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Authors: | Mitsui Shinichi; Sugiura Masahiro |
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Institution: | Center for Gene Research, Nagoya University Nagoya, 464-01 Japan |
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Abstract: | A cytokinin-binding protein complex was purified 700-fold fromleaves of tobacco (Nicotiana sylvestris). The purification procedureconsisted of four chromatographic steps on columns of DEAE-cellulose,Mono Q, Phenyl Superose and Superose 12, respectively. The purifiedcytokinin-binding protein complex behaved as a 130-kDa globularprotein on gel filtration. This complex contains two proteinspecies whose molecular masses are estimated to be 57 kDa and36 kDa. Binding to benzyl8-14C]adenine was inhibited by adenine,ATP, zeatin and cAMP but not by indoleacetic acid. Scatchardanalysis indicated the existence of at least two cytokinin-bindingsites in the purified complex. The dissociation constant forthe high-affinity site was 2.1 10-5 M. (Received October 19, 1992; Accepted February 27, 1993) |
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