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Glycosylation analysis of gel‐separated proteins
Author(s) -
Küster Bernhard,
Krogh Thomas N.,
Mørtz Ejvind,
Harvey David J.
Publication year - 2001
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200102)1:2<350::aid-prot350>3.0.co;2-7
Subject(s) - glycosylation , biochemistry , proteomics , chemistry , computational biology , glycoprotein , proteome , biology , gene
Beyond the identification of proteins involved in a particular physiological situation, many aspects of proteomics require more detailed characterization of the proteins involved. Post‐translational modifications (PTMs) of proteins are a common means to target proteins, regulate their activities and to mediate communication between proteins and cells. Owing to the much higher analytical complexity of glycan analysis compared to e. g. protein identification, PTM analysis in general and glycosylation analysis in particular is largely neglected in proteomics. In this review, the current technological status of global and site‐specific glycosylation analysis of gel‐separated proteins is described and the way in which the available technology can be employed in proteomics is critically discussed.