Main > PROTEINS > Proteomics > Glycosylated Protein (GlycoProtein) > O-Linked Beta-N-AcetylGlucosAmine > Org.: USA. U (Detectiom Technique) > NPLS Contents-2

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Method identifies O-linked glycans

Proteins containing glycan sugar substituents attached through an oxygen linkage at either serine or threonine are difficult to analyze because of a lack of suitable methods. The available methods are either not specific to the O-linked glycans or so harsh that they damage the protein. Carolyn R. Bertozzi, a chemistry professor at the University of California, Berkeley, and her colleagues describe a method for labeling mucin-type O-linked glycans, which are linked to the protein through an N-acetylgalactosamine, or GalNAc, residue [Proc. Natl. Acad. Sci. USA, published online, http://www.pnas.org/cgi/doi/10.1073/pnas.2335201100]. An azide analog of GalNAc is metabolically incorporated into the glycoproteins. The azides can then be labeled with a phosphine probe via the Staudinger ligation. The phosphine probe allows the glycoproteins to be separated and enriched for proteomic analysis. Bertozzi and her colleagues have shown that the azide analogs can be incorporated into glycoproteins of mammalian cells; they hope to use the technique in live animals next.




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