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

Conference · Tue May 01 00:00:00 EDT 1990 · Plant Physiology, Supplement; (USA)

OSTI ID:5841563

Cosio, E G; Waldmueller, T; Frey, T; Ebel, J ^[1]

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1. Biologisches Institut II der Universitat Freiburg (West Germany)

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.

• OSTI ID: 5841563
• Report Number(s): CONF-9007196-; CODEN: PPYSA
• Journal Information: Plant Physiology, Supplement; (USA), Vol. 93:1; Conference: Annual meeting of the American Society of Plant Physiologists, Indianapolis, IN (USA), 29 Jul - 2 Aug 1990; ISSN 0079-2241
• Country of Publication: United States
• Language: English

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IODINE COMPOUNDS
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IODINE 125
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550201* - Biochemistry- Tracer Techniques