Purification of a Soluble Cytockinin-binding Protein from Etiolated Mung Bean Seedlings
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概要
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A cytokinin-binding protein (CBP) was purified from a crude extract of etiolated mung bean seedlings by a protocol involving affinity chromatography on benzyladenine-linked Sepharose 4B, ion exchange chromatography on DEAE-Sephadex A50,and gel filtration on Sphacryl S-400. The molecular weight was estimatd to be about 200,000 by gel filtration. CBP appeared as two bands corresponding to molecular weights of about 45,000 and 48,000 on SDS-polyacrylamide gel electrophoresis. The dissociation constant for benzyladenine was 7.5 x 1^<-7> M. ^<14>C-Benzyladenine-binding to CBP was reversible and could be inhibited by the addition of kinetin or trans-zeatin. Adenine, AMP, and ADP had no inhibitory effect on the binding of^<14>C-benzyladenine to CBP but the addition of ATP to the assay mixture enhanced the binding.
- 社団法人日本農芸化学会の論文
- 1992-03-23
著者
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Sakai Shingo
Institute For Biochemical Regulation Faculty Of Agriculture Nagoya University
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KAMEI Naoki
Institute of Biological Sciences, University of Tsukuba
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Kamei Naoki
Institute Of Biological Sciences University Of Tsukuba
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