A Soluble High Affinity Auxin-Binding Protein from Pea Apex
- authored by
- 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 KD = 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.
- Organisation(s)
-
Institute of Plant Genetics
- Type
- Article
- Journal
- Journal of plant physiology
- Volume
- 147
- Pages
- 132-138
- No. of pages
- 7
- ISSN
- 0176-1617
- Publication date
- 1995
- Publication status
- Published
- Peer reviewed
- Yes
- ASJC Scopus subject areas
- Physiology, Agronomy and Crop Science, Plant Science
- Electronic version(s)
-
https://doi.org/10.1016/S0176-1617(11)81425-2 (Access:
Closed)
