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Elution of glycoproteins from replicas of sodium dodecyl sulfate‐polyacrylamide gel electrophoresis gels
Author(s) -
Szewczyk Boguslaw,
Pilat Zbigniew,
BienkowskaSzewczyk Krystyna,
Summers Donald F.
Publication year - 1998
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.1150190214
Subject(s) - chromatography , chemistry , sodium dodecyl sulfate , elution , gel electrophoresis , glycoprotein , polyacrylamide gel electrophoresis , electrophoresis , sodium , molecular weight size marker , membrane , glycan , gel electrophoresis of proteins , biochemistry , organic chemistry , enzyme
A method for the elution of glycoproteins from sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) replicas of gels on polyvinylidene difluoride (PVDF) membranes is described. Ten model glycoproteins were resolved by SDS‐PAGE and then electrotransferred onto PVDF membranes. After reversible staining, glycoprotein bands were eluted with a mixture of SDS/Triton X‐100 at pH 9 or with a mixture of guanidinium hydrochloride/lysophosphatidylcholine at neutral pH. For both types of eluents, the final recoveries ranged from over 30% to about 80%. Good recoveries and mild conditions of elution render the method applicable for the structural elucidation of glycan chains.