Purification and Properties of an Auxin-Binding Protein from the Shoot Apex of Peach Tree |
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Authors: | Ohmiya Akemi; Kikuchi Motoyuki; Sakai Shingo; Hayashi Tateki |
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Institution: | 1Department of Breeding, Fruit Tree Research Station, Ministry of Agriculture, Forestry and Fisheries Tsukuba, Ibaraki, 305 Japan
2Institute of Biological Science, University of Tsukuba Tsukuba, Ibaraki, 305 Japan |
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Abstract: | A soluble auxin-binding protein was purified from the shootapices 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 tobe 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-Dwas calculated to be 4.1 105 M and the specific bindingof 2,4-D at saturating concentration was 42 nmol (mg protein)1.The binding of 14C]-2,4-D to the protein was reversible andwas inhibited by IAA, 1-naphthylacetic acid and p-chlorophenoxyisobutyricacid. (Received June 25, 1992; Accepted October 20, 1992) |
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