Abstract
Summary A soluble auxin-binding protein (ABP 44 ) from etiolated seedlings of Pisum sativum L. has been purified. It was detected in the apex but not in the basal, non-dividing parts of the pea epicotyls. Different set-ups of affinity chromatography were found to be powerful tools for the purification and characterization of ABP 44 . The determination of the binding kinetics was done using equilibrium dialysis binding tests. The modifications and improvements of the equilibrium binding assay, described previously (Reinard and Jacobsen, 1989), allowed the assignment of auxin binding activity to a purified soluble protein (ABP 44 ) with a dissociation constant of K D = 7.5 nM for the naturally occurring IAA. The data presented indicate that ABP 44 binds active auxins both with a high affinity and great specificity.
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