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Glycobiology and proteomics: Is mass spectrometry the holy grail?
Author(s) -
Packer Nicolle H.,
Harrison Mathew J.
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.1150191105
Subject(s) - isoelectric point , glycan , glycobiology , chemistry , mass spectrometry , glycosylation , proteomics , glycomics , glycoprotein , chromatography , isoelectric focusing , biochemistry , computational biology , biology , gene , enzyme
One characteristic of glycoproteins is that they are separated by two‐dimensional electrophoresis (2‐D PAGE) into typical ‘trains’ of protein spots which separate on the basis of different isoelectric point (p I ) and/or molecular mass. The pattern of these trains often varies in development and disease. While the isoforms differ both in the number of sites of glycosylation and the types of carbohydrate attached to the protein, classical methods of glycan analysis are insensitive at the levels typically separated by 2‐D PAGE. Developments in mass spectrometry technologies have enabled the characterization of most of the oligosaccharide attributes to be determined on picomole amounts of protein. These techniques are beginning to allow the glycoform heterogeneity on 2‐D separated glycoproteins to be analyzed.