Glycosylation analysis of gel-separated proteins.
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.
Küster
B
B
MDS Protana, Odense, Denmark. kuster@cellzome.de
Krogh
T N
TN
Mørtz
E
E
Harvey
D J
DJ
D000818:Animals; D002240:Carbohydrate Sequence; D004591:Electrophoresis, Polyacrylamide Gel / Q000266:history / Q000379:methods*; D006023:Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification*; D006026:Glycoside Hydrolases; D006031:Glycosylation; D049673:History, 20th Century; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D020543:Proteome; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D006023:Glycoproteins; D011134:Polysaccharides; D020543:Proteome; D006026:Glycoside Hydrolases