A Soluble High Affinity Auxin-Binding Protein from Pea Apex

verfasst von

Thomas Reinard, Hans Jörg Jacobsen

Abstract

A soluble auxin-binding protein (ABP₄₄) 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 ABP₄₄. 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 (ABP₄₄) with a dissociation constant of K_D = 7.5 nM for the naturally occurring IAA. The data presented indicate that ABP₄₄ binds active auxins both with a high affinity and great specificity.

Organisationseinheit(en)

Institut für Pflanzengenetik

Typ

Artikel

Journal

Journal of plant physiology

Band

147

Seiten

132-138

Anzahl der Seiten

7

ISSN

0176-1617

Publikationsdatum

1995

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Physiologie, Agronomie und Nutzpflanzenwissenschaften, Pflanzenkunde

Elektronische Version(en)

https://doi.org/10.1016/S0176-1617(11)81425-2 (Zugang: Geschlossen)