Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 132-138 |
| Seitenumfang | 7 |
| Fachzeitschrift | Journal of plant physiology |
| Jahrgang | 147 |
| Ausgabenummer | 1 |
| Publikationsstatus | Veröffentlicht - 1995 |
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Physiologie
- Agrar- und Biowissenschaften (insg.)
- Agronomie und Nutzpflanzenwissenschaften
- Agrar- und Biowissenschaften (insg.)
- Pflanzenkunde
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in: Journal of plant physiology, Jahrgang 147, Nr. 1, 1995, S. 132-138.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - A Soluble High Affinity Auxin-Binding Protein from Pea Apex
AU - Reinard, Thomas
AU - Jacobsen, Hans Jörg
N1 - Funding Information: This work was supported by grants from the Heinrich-HertzStiftung NRW and Graduierten Forderung NRW to T.R. and fi nanced by the Deutsche Forschungsgemeinschaft Oa 318/5-3) and partly through a Bundesministerium fUr Forschung und Technologie (BMFT) grant (BEO 0318969C) to H.-J. J.
PY - 1995
Y1 - 1995
N2 - 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.
AB - 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.
KW - 2,3,5-triiodobenzoic acid
KW - 2,4-D
KW - 2,4-dichlorophenoxyacetic acid
KW - 4-0H-PAA
KW - 4-hydroxy-phenylacetic acid
KW - 5-azido-[7-H]indole-3-acetic acid
KW - ABP
KW - apex
KW - Auxin
KW - auxin binding protein
KW - auxin-binding protein
KW - azido-IAA
KW - IAA
KW - indole-3-acetic acid
KW - NAA
KW - naphthalene acetic acid
KW - naphthylphthalamic acid
KW - NPA
KW - PAA
KW - pea
KW - phenylacetic acid
KW - TIBA
UR - http://www.scopus.com/inward/record.url?scp=0029175534&partnerID=8YFLogxK
U2 - 10.1016/S0176-1617(11)81425-2
DO - 10.1016/S0176-1617(11)81425-2
M3 - Article
AN - SCOPUS:0029175534
VL - 147
SP - 132
EP - 138
JO - Journal of plant physiology
JF - Journal of plant physiology
SN - 0176-1617
IS - 1
ER -