| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5278245 | Tetrahedron Letters | 2008 | 4 Pages |
Abstract
A new strategy to tag glycoproteins carrying terminal GlcNAc was developed using commercially available bovine β-1,4-galactosyltransferase (GalT) and UDP-6-azidogalactose. The azide function was then allowed to react via a biotinylated Staudinger-Bertozzi probe demonstrating the usefulness of such a procedure to tag any glycoprotein possessing a N-acetylglucosamine terminal residue from any type of cell lysate.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Michaël Bosco, Sophie Le Gall, Christophe Rihouey, Samuel Couve-Bonnaire, Muriel Bardor, Patrice Lerouge, Xavier Pannecoucke,