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Permanent link (DOI): https://doi.org/10.7939/R38H1W

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Characterization of glycoproteins and oligosaccharides using mass spectrometry Open Access

Descriptions

Other title
Subject/Keyword
Glycoproteins
Mass spectrometry
Oligosaccharide gas phase dissociations
Tandem MS
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Fentabil, Messele
Supervisor and department
Klassen, John (Department of Chemistry)
Examining committee member and department
Lucy, Charles (Department of Chemistry)
Szymanski, Christine (Department of Biological Sciences)
Department
Department of Chemistry
Specialization

Date accepted
2010-08-30T20:41:07Z
Graduation date
2010-11
Degree
Master of Science
Degree level
Master's
Abstract
This thesis describes the application of mass spectrometry (MS) to glycoprotein and oligosaccharide analysis. Glycosylated proteins are involved in cell-cell and cell-matrix recognition. Applications of trypsin and proteinase K to hydrolyze glycoproteins into glycopeptides that are compatible with MS and MS/MS analysis are investigated. For successful site-specific analysis of glycans, glycopeptides with short peptide (3-8 residues) are needed. Although trypsin is an important enzyme for protein identification, proteinase K is superior for site-specific glycan analysis due to its potential to hydrolyze every glycoprotein to short glycopeptides. The gas-phase dissociation pathways, kinetics and energetics of protonated oligosaccharides are described. The oligosaccharides dissociate via cleavage at the glycosidic linkages during thermal activation. Using double resonance experiments, it was established that oligosaccharides undergo sequential and parallel fragmentation reactions. Furthermore, dissociation of product ions to secondary ions was confirmed. Arrhenius activation parameters, Ea and A for protonated alpha- and beta-linked D-glucopyranose oligosaccharides are reported.
Language
English
DOI
doi:10.7939/R38H1W
Rights
License granted by Messele Fentabil (fentabil@ualberta.ca) on 2010-08-27T20:40:27Z (GMT): Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of the above terms. The author reserves all other publication and other rights in association with the copyright in the thesis, and except as herein provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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File title: Full Thesis combined June 30
File author: Messele Fentabil
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