Purification and Properties of an Auxin-Binding Protein from the Shoot Apex of Peach Tree
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概要
- 論文の詳細を見る
A soluble auxin-binding protein was purified from the shoot apices of peach trees by chromatography on columns of CM-Toyopearl, Sephacryl S-200, 2,4-D-linked-Sepharose 4B and ConA-Sepharose. The molecular mass of the purified protein was estimated to be about 100 kDa. After electrophoresis on a denaturing gel, the protein gave a single band with a molecular mass of 20 kDa. From Scatchard analyses, the dissociation constant for 2,4-D was calculated to be 4. 1×10^<-5> M and the specific binding of 2,4-D at saturating concentration was 42 nmol (mg protein)^<-1>. The binding of [^<14>C]-2,4-D to the protein was reversible and was inhibited by IAA, 1-naphthylacetic acid and p-chlorophenoxyisobutyric acid.
- 日本植物生理学会の論文
著者
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HAYASHI Tateki
Department of Food Science and Technology, Nagoya University
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Hayashi T
National Institute Of Fruit Tree Science Ministry Of Agriculture Forestry And Fisheries
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OHMIYA Akemi
Department of Breeding, Fruit Tree Research Station, Ministry of Agriculture, Forestry and Fisheries
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KIKUCHI Motoyuki
Department of Breeding, Fruit Tree Research Station, Ministry of Agriculture, Forestry and Fisheries
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SAKAI Shingo
Institute of Biological Science, University of Tsukuba
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Hayashi Tateki
Department Of Food Science & Technology Faculty Of Agriculture Nagoya University
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Ohmiya A
National Institute Of Floricultural Science
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Hakoyama Tsuneo
Department Of Plant Sciences National Institute Of Agrobiological Sciences
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Kikuchi Motoyuki
National Institute Of Fruit Tree Science Ministry Of Agriculture Forestry And Fisheries:(present Add
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Sakai Shingo
Institute Of Biological Science University Of Tsukuba
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Sakai Shingo
Institute For Biochemical Regulation Faculty Of Agriculture Nagoya University
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