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Solubilization of soybean membrane binding sites for fungal β‐glucans that elicit phytoalexin accumulation
Author(s) -
Cosio Eric G.,
Frey Thomas,
Ebel Jürgen
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80256-i
Subject(s) - chromatofocusing , membrane , chemistry , glucan , phytoalexin , biochemistry , phosphorylcholine , micelle , gel permeation chromatography , chromatography , microsome , affinity chromatography , organic chemistry , in vitro , size exclusion chromatography , aqueous solution , enzyme , resveratrol , polymer
Soybean membranes contain high‐affinity binding sites for fungal β‐glucans. These sites may play a role in the recognition by soybean tissues of fungal phytoalexin elicitors. We have solubilized β‐glucan‐binding activity from microsomal membranes using two C 12 ,‐alkyl zwitterionic detergents, Zwittergent 3‐12 (ZW 3‐12) and the lysolecithin analog l‐dodecyl‐2‐deoxy‐phosphorylcholine (ES12H). The solubilized binding sites displayed identical affinity for β‐glucans as that found in membranes ( K d = 11‐34 nM). Detergent‐protein micelles with glucan binding activity eluted with approximate M r values of 3 in ZW 3‐12 and 380000 in ES12H in gel permeation chromatography. Maximal binding activity eluted from a chromatofocusing column in the pH range between 6.2 and 6.6 with both ES12H and ZW 3‐12, suggesting an apparent p I close to neutral.