An auxin-binding protein with high affinity for 2,4-D and IAA was purified from the extract of etiolated mung bean seedlings by affinity chromatography on 2,4-D-linked Sepharose 4B and by gel nitration on Sepharose 4B. Its molecular weight was estimated to be about 390,000 by gel nitration on Sepharose 4B and it consisted of two different subunits with molecular weights of about 47,000 and 15,000. This protein had no ribulose-l,5-bisphosphate carboxylase activity. Its dissociation constants for 2,4-D and IAA were 9.3×10−6Mand 3.2×10−6M, respectively, as determined by Scatchard's m
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