Purification and Properties of Cytokinin-Binding Proteins from Tobacco Leaves
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概要
- 論文の詳細を見る
A cytokinin-binding protein complex was purified 700-fold from leaves of tobacco (Nicotiana sylvestris). The purification procedure consisted of four chromatographic steps on columns of DEAE-cellulose, Mono Q, Phenyl Superose and Superose 12, respectively. The purified cytokinin-binding protein complex behaved as a 130-kDa globular protein on gel filtration. This complex contains two protein species whose molecular masses are estimated to be 57 kDa and 36 kDa. Binding to benzyl[8-^<14>C]adenine was inhibited by adenine, ATP, zeatin and CAMP but not by indoleacetic acid. Scatchard analysis indicated the existence of at least two cytokinin-binding sites in the purified complex. The dissociation constant for the high-affinity site was 2.1×10^<-5> M.
- 日本植物生理学会の論文
著者
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SUGIURA Masahiro
Center for Gene Research, Nagoya University
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Sugiura Masahiro
Center For Gene Res. Nagoya Univ.
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Sugiura Masahiro
Center For Gene Research Nagoya University
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MITSUI Shinichi
Center for Gene Research, Nagoya University
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Mitsui Shinichi
Center For Gene Research Nagoya University
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Sugiura Masahiro
Center For Gene Res Nagoya University
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