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Plant and Cell Physiology, 1985, Vol. 26, No. 1 185-192
© 1985

Article

Auxin-Binding Protein in Etiolated Mung Bean Seedlings: Purification and Properties of Auxin-Bindmg Protein-II

Shingo Sakai

Laboratory of Cell Biochemistry, Faculty of Science, Saitama University Urawa 338, Japan

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 amrnonium sulfate precipitation and equilibrium dialysis were 9.5×10–6 M and 1.1×10–5 M, respectively. 14C-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.

(Received September 5, 1984; Accepted November 5, 1984)
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