How to find, identify and quantitate the sugars on proteins
- 1 February 1997
- journal article
- Published by Springer Nature in Nature
- Vol. 385 (6616) , 557-559
- https://doi.org/10.1038/385557a0
Abstract
A new sequenator allows the identification, quantification and characterization of sites of glycosylation on proteins, making it possible to analyse the glycosylation at serine and threonine sites in mucin-like domains.Keywords
This publication has 12 references indexed in Scilit:
- Getting the glycosylation right: Implications for the biotechnology industryNature Biotechnology, 1996
- In MemoriamASA News, 1996
- The Amino Acid at the X Position of an Asn-X-Ser Sequon Is an Important Determinant of N-Linked Core-glycosylation EfficiencyJournal of Biological Chemistry, 1996
- Identification and Characterization of Glycosylated Phenylthiohydantoin Amino AcidsPublished by Springer Nature ,1995
- Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine κ-caseinGlycobiology, 1994
- Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin AGlycobiology, 1993
- O-Linked fucose and other post-translational modifications unique to EGF modulesGlycobiology, 1993
- Selective identification and differentiation of N‐and O‐linked oligosaccharides in glycoproteins by liquid chromatography‐mass spectrometryProtein Science, 1993
- Integration of mass spectrometry in analytical biotechnologyAnalytical Chemistry, 1991
- Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: The identification of Xaa-Pro-Xaa-Xaa as a motif for Thr-O-glycosylationBiochemical and Biophysical Research Communications, 1991