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Visualization of barley β‐glucan degrading isozymes after gel isoelectric focusing
Author(s) -
Menteur Sophie,
Jestin Louis,
Risacher Thierry,
Branlard Gérard
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501601171
Subject(s) - isoelectric focusing , hordeum vulgare , congo red , glucan , hydrolysis , isozyme , isoelectric point , chromatography , chemistry , polyacrylamide gel electrophoresis , staining , biology , biochemistry , enzyme , botany , poaceae , organic chemistry , genetics , adsorption
A simple method to study the polymorphism of barley ( Hordeum vulgare L.) β‐(1–3, 1–4)‐glucanases (specific enzymes of barley β‐glucan hydrolysis) is described. Proteins of a crude extract of germinated barley kernels were separated in an immobilized pH gradient in two pH ranges (pH 3–10.5 and pH 4–7). β‐glucanases were visualized by contact printing with a polyacrylamide gel containing β‐glucan or lichenan. Patterns of β‐glucanases were revealed by staining with Congo Red with resultant clear zones on a stained background. Various conditions of germination, extraction and visualization were investigated. New isozyme bands could be detected and their nature and origin discussed.