11-08-2016, 09:14 PM
Glycan capacities are typically controlled by the structures of the oligosaccharides, which are covalently appended to proteins fundamentally at 2 basic themes: the amide gathering of an asparagine (N-glycans) or the hydroxyl bunch on serine or threonine (O-glycans). As a result of the differing qualities of the oligosaccharides, even glycosylation at a solitary site can produce significant heterogeneity of the mass and charge of glycoproteins. Albeit distinctive methodologies for N-glycans investigation have been depicted, as a rule these techniques depend on enzymatic arrival of N-glycans from the protein by PNGase F, and induction of discharged glycans, because of the absence of inborn chromophores, with a fluorescent naming before examination.
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http://www.creative-proteomics.com/servi...alysis.htm