We have developed a method for monitoring the \(\mathrm{N}\). glycosylation of recombinant glycoproteins directly from conditioned medium samples. Proteins in the conditioned medium are separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electroblotted onto polyvinylidene fluo
Monitoring the N-glycosylation of plant glycoproteins by fluorophore-assisted carbohydrate electrophoresis
✍ Scribed by Muriel Bardor; Marion Cabanes-Macheteau; Loïc Faye; Patrice Lerouge
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 171 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0173-0835
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A sensitive and facile method is described to identify the glycosylation sites and site-spedfic heterogeneity in the carbohydrate attached to glycoproteins. In this procedure, the peptide backbone of the glycoprotein is cleaved enzymatically. The resulting peptide/glycopeptide mixture is divided int
Previously, a combined use of fast atom bombardment (FAB) mass spectrometry and peptide N-glycosidase F, an enzyme that cleaves the beta-aspartylglycosylamine linkage of Asn-linked carbohydrates, was successfully applied to identification of N-glycosylation sites in a glycoprotein with the known or