Abstract
Gibberellin-binding proteins (GBPs) were isolated from a crude extract of etiolated maize seedlings by affinity chromatography on gibberellin A3(GA3)-linked enhance-aminohexyl(EAH)-Sepharose 4B. The isolated proteins had a binding activity for [3H]-GA4. The binding site with dissociation constant of 0.5 μM for GA4 was detected in the proteins by the binding assay with the procedures of ammonium sulfate precipitation. The binding of [3H]-GA4 to GBPs was reversible and could be inhibited by the addition of GA1 and GA3. An inactive gibberellin, GA13, had no inhibitory effect on the binding of [3H]-GA4 to GBPs.
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