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Monitoring the N ‐glycosylation of plant glycoproteins by fluorophore‐assisted carbohydrate electrophoresis
Author(s) -
Bardor Muriel,
CabanesMacheteau Marion,
Faye Loïc,
Lerouge Patrice
Publication year - 2000
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(20000701)21:12<2550::aid-elps2550>3.0.co;2-g
Subject(s) - glycan , glycoprotein , glycosylation , fluorophore , chemistry , concanavalin a , chromatography , biochemistry , electrophoresis , gel electrophoresis , affinity electrophoresis , carbohydrate , mannose , polyacrylamide gel electrophoresis , glycoconjugate , affinity chromatography , enzyme , fluorescence , in vitro , physics , quantum mechanics
We have evaluated the efficiency of a fast, simple and efficient method, fluorophore‐assisted carbohydrate electrophoresis (FACE), for the characterization of plant N ‐linked glycans. After their enzymatic release from plant glycoproteins, N ‐glycans were reductively aminated to the charged fluorophore 8‐aminonaphthalene‐1, 3, 6‐trisulfonic acid (ANTS) and separated using high resolution polyacrylamide gel electrophoresis. In addition, an affinity purification procedure using concanavalin A was developed for separation of ANTS‐labeled high‐mannose‐type N ‐glycans from other plant oligosaccharides.