N-glycosylation site mapping of human serotransferrinby serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy
- 1 October 1992
- journal article
- Published by Elsevier in Analytical Biochemistry
- Vol. 206 (1) , 53-63
- https://doi.org/10.1016/s0003-2697(05)80010-7
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Integration of mass spectrometry in analytical biotechnologyAnalytical Chemistry, 1991
- Presence of fucosylated triantennary, tetraantennary and pentaantennary glycans in transferrin synthesized by the human hepatocarcinoma cell line Hep G2European Journal of Biochemistry, 1989
- Physiological significance of the marked increased branching of the glycans of human serotransferrin during pregnancyBiochemical Journal, 1989
- Structural fingerprinting of Asn-linked carbohydrates from specific attachment sites in glycoproteins by mass spectrometry: application to tissue plasminogen activatorBiochimie, 1988
- Use of N-glycanase to release asparagine-linked oligosaccharides for structural analysisAnalytical Biochemistry, 1987
- Carbohydrate mapping by mass spectrometry: A novel method for identifying attachment sites of asn-linked sugars in glycoproteinsAnalytical Biochemistry, 1986
- Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase FBiochemistry, 1985
- Primary structure of two sialylated triantennary glycans from human serotransferrinFEBS Letters, 1985
- The structure of the asialo‐carbohydrate units of human serotransferrin as proven by 360 MHz proton magnetic resonance spectroscopyFEBS Letters, 1977
- Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrinFEBS Letters, 1975