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Title: Soybean. beta. -glucan binding sites display maximal affinity for a heptaglucoside phytoalexin-elicitor

Abstract

The affinity of soybean {beta}-glucan-binding sites for a synthetic heptaglucan elicitor was tested in a ligand-competition assay against a {sup 125}I-labeled 1,3-1,6-{beta}-glucan preparation (avg. DP=20). Half-maximal displacement of label (IC{sub 50}) was obtained at 9nM heptaglucan, the highest affinity of all fractions tested to date. Displacement followed a uniform sigmoidal pattern and was complete at 1{mu}M indicating access of heptaglucan to all sites available to the labeled elicitor. A mathematical model was used to predict IC{sub 50} values according to the DP of glucan fragments obtained from fungal cell walls. The lowest IC{sub 50} predicted by this model is 3nM. Binding affinity of the glucans was compared with their elicitor activity in a bioassay.

Authors:
; ; ;  [1]
  1. Biologisches Institut II der Universitat Freiburg (West Germany)
Publication Date:
OSTI Identifier:
5841563
Report Number(s):
CONF-9007196-
Journal ID: ISSN 0079-2241; CODEN: PPYSA
Resource Type:
Conference
Journal Name:
Plant Physiology, Supplement; (USA)
Additional Journal Information:
Journal Volume: 93:1; Conference: Annual meeting of the American Society of Plant Physiologists, Indianapolis, IN (USA), 29 Jul - 2 Aug 1990; Journal ID: ISSN 0079-2241
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; IODINE COMPOUNDS; BIOCHEMICAL REACTION KINETICS; FUNGI; GLYCINE HISPIDA; IODINE 125; LIGANDS; MATHEMATICAL MODELS; STARCH; TRACER TECHNIQUES; BETA DECAY RADIOISOTOPES; CARBOHYDRATES; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; HALOGEN COMPOUNDS; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; LEGUMINOSAE; MAGNOLIOPHYTA; MAGNOLIOPSIDA; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; PLANTS; POLYSACCHARIDES; RADIOISOTOPES; REACTION KINETICS; REAGENTS; SACCHARIDES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Cosio, E G, Waldmueller, T, Frey, T, and Ebel, J. Soybean. beta. -glucan binding sites display maximal affinity for a heptaglucoside phytoalexin-elicitor. United States: N. p., 1990. Web.
Cosio, E G, Waldmueller, T, Frey, T, & Ebel, J. Soybean. beta. -glucan binding sites display maximal affinity for a heptaglucoside phytoalexin-elicitor. United States.
Cosio, E G, Waldmueller, T, Frey, T, and Ebel, J. 1990. "Soybean. beta. -glucan binding sites display maximal affinity for a heptaglucoside phytoalexin-elicitor". United States.
@article{osti_5841563,
title = {Soybean. beta. -glucan binding sites display maximal affinity for a heptaglucoside phytoalexin-elicitor},
author = {Cosio, E G and Waldmueller, T and Frey, T and Ebel, J},
abstractNote = {The affinity of soybean {beta}-glucan-binding sites for a synthetic heptaglucan elicitor was tested in a ligand-competition assay against a {sup 125}I-labeled 1,3-1,6-{beta}-glucan preparation (avg. DP=20). Half-maximal displacement of label (IC{sub 50}) was obtained at 9nM heptaglucan, the highest affinity of all fractions tested to date. Displacement followed a uniform sigmoidal pattern and was complete at 1{mu}M indicating access of heptaglucan to all sites available to the labeled elicitor. A mathematical model was used to predict IC{sub 50} values according to the DP of glucan fragments obtained from fungal cell walls. The lowest IC{sub 50} predicted by this model is 3nM. Binding affinity of the glucans was compared with their elicitor activity in a bioassay.},
doi = {},
url = {https://www.osti.gov/biblio/5841563}, journal = {Plant Physiology, Supplement; (USA)},
issn = {0079-2241},
number = ,
volume = 93:1,
place = {United States},
year = {Tue May 01 00:00:00 EDT 1990},
month = {Tue May 01 00:00:00 EDT 1990}
}

Conference:
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