Details
| Original language | English |
|---|---|
| Pages (from-to) | 874-878 |
| Number of pages | 5 |
| Journal | Plant and Cell Physiology |
| Volume | 39 |
| Issue number | 8 |
| Publication status | Published - 1 Aug 1998 |
Abstract
Several approaches were successfully performed to directly assign and characterize auxin binding of ABP44 in gel. The 44 kDa high affinity auxin binding protein ABP44 from pea was tested for its ability to bind 5-azido-[7-3H]-IAA in photoaffinity labeling experiments. Competition experiments with several auxin analogues confirm data published previously (Reinard and Jacobsen 1995). Critical reflections of the limitations of 'the method are also discussed. Immunostaining using the antibody D16 (Napier and Venis 1992), which is directed against the putative binding site of ABP1, revealed that ABP44's auxin binding site is at least partially related to the corresponding site of ABP1. Nevertheless, both proteins do not share any further immunological relationships. Our results with D16 recommend a careful reconsideration of data published by other authors. Furthermore, a 80 kDa, dimeric glutathione dependent formaldehyde dehydrogenase (FDH) from mung bean, described recently, was found to be different from ABP44. In contrast to the described FDH, ABP44 exhibited no FDH activity.
Keywords
- Auxin binding protein, Formaldehyde dehydrogenase, Photoaffinity labeling, Pisum sativum
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Physiology
- Agricultural and Biological Sciences(all)
- Plant Science
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Plant and Cell Physiology, Vol. 39, No. 8, 01.08.1998, p. 874-878.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Assignment of the Auxin Binding Abilities of ABP44 in Gel
AU - Reinard, Thomas
AU - Achmus, Heike
AU - Walther, Antje
AU - Rescher, Ursula
AU - Klämbt, Dieter
AU - Jacobsen, Hans Jörg
N1 - Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft to T.R. (Re 1012/3-2). We thank Dr. Alan Jones, University of North Carolina at Chapel Hill, for providing the 5-azido-[7-3H]IAA and Dr. Richard Napier, Horticulture Research International, East Mailing, Kent, U.K. We thank Neera Tewari for practical help in the preparation of the manuscript.
PY - 1998/8/1
Y1 - 1998/8/1
N2 - Several approaches were successfully performed to directly assign and characterize auxin binding of ABP44 in gel. The 44 kDa high affinity auxin binding protein ABP44 from pea was tested for its ability to bind 5-azido-[7-3H]-IAA in photoaffinity labeling experiments. Competition experiments with several auxin analogues confirm data published previously (Reinard and Jacobsen 1995). Critical reflections of the limitations of 'the method are also discussed. Immunostaining using the antibody D16 (Napier and Venis 1992), which is directed against the putative binding site of ABP1, revealed that ABP44's auxin binding site is at least partially related to the corresponding site of ABP1. Nevertheless, both proteins do not share any further immunological relationships. Our results with D16 recommend a careful reconsideration of data published by other authors. Furthermore, a 80 kDa, dimeric glutathione dependent formaldehyde dehydrogenase (FDH) from mung bean, described recently, was found to be different from ABP44. In contrast to the described FDH, ABP44 exhibited no FDH activity.
AB - Several approaches were successfully performed to directly assign and characterize auxin binding of ABP44 in gel. The 44 kDa high affinity auxin binding protein ABP44 from pea was tested for its ability to bind 5-azido-[7-3H]-IAA in photoaffinity labeling experiments. Competition experiments with several auxin analogues confirm data published previously (Reinard and Jacobsen 1995). Critical reflections of the limitations of 'the method are also discussed. Immunostaining using the antibody D16 (Napier and Venis 1992), which is directed against the putative binding site of ABP1, revealed that ABP44's auxin binding site is at least partially related to the corresponding site of ABP1. Nevertheless, both proteins do not share any further immunological relationships. Our results with D16 recommend a careful reconsideration of data published by other authors. Furthermore, a 80 kDa, dimeric glutathione dependent formaldehyde dehydrogenase (FDH) from mung bean, described recently, was found to be different from ABP44. In contrast to the described FDH, ABP44 exhibited no FDH activity.
KW - Auxin binding protein
KW - Formaldehyde dehydrogenase
KW - Photoaffinity labeling
KW - Pisum sativum
UR - http://www.scopus.com/inward/record.url?scp=0032143586&partnerID=8YFLogxK
U2 - 10.1093/oxfordjournals.pcp.a029447
DO - 10.1093/oxfordjournals.pcp.a029447
M3 - Article
C2 - 9787462
AN - SCOPUS:0032143586
VL - 39
SP - 874
EP - 878
JO - Plant and Cell Physiology
JF - Plant and Cell Physiology
SN - 0032-0781
IS - 8
ER -