Auxin-Binding Protein in Etiolated Mung Bean Seedlings : Purification and Properties of Auxin-Binding Protein-II
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概要
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An auxin-binding protein (ABP-II) was purified from the extract of etiolated mung bean seedlings by affinity chromatography on 2,4-D-linked Sepharose 4B and by gel filtration on Sepharose 4B and Sephacryl S-200. The molecular weight was estimated to be about 190,000 by gel filtration on Sephacryl S-200. ABP-II gave a single band corresponding to a molecular weight of about 48,000 on SDS-polyacrylamide gel electrophoresis. The dissociation constants of ABP-II for 2,4-D determined by ammonium sulfate precipitation and equilibrium dialysis were 9.5 × 10^<-6> M and 1.1 × 10^<-5> M, respectively. ^<14>C-2,4-D-binding to ABP-II was reversible and inhibited by addition of IAA, naphthalene-1-acetic acid, 2,4,5-trichlorophenoxyacetic acid or p-chlorophenoxyisobutylic acid to the assay mixture.
- 日本植物生理学会の論文
著者
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Sakai S
Institute Of Biological Sciences University Of Tsukuba
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Sakai Shingo
Laboratory of Cell Biochemistry, Faculty of Science, Saitama University
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Sakai Shingo
Laboralory Of Cell Biochemistry Faculty Of Science Saitama University
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