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Jessica M. Risley
University of British Columbia
Proteins with attached sugars can be used to treat illnesses. It is important to study the sugar component of the protein because the sugars are often complex and can cause negative immune system reactions. Glycans are the complex branched oligosaccharides which are covalently linked to protein molecules. Characterization of the glycan component of glycoproteins is challenging due to microheterogeneity, but necessary as glycans can cause negative immune system reactions.
Erythropoietin is a glycoprotein hormone that stimulates the production of red blood cells and is used as a therapy for anemic patients. However, erythropoietin is also used as a doping agent in sports to boost performance by increasing the oxygen-carrying capacity of blood. Techniques for studying the glycans of erythropoietin and for differentiating between endogenous and exogenous erythropoietin are of interest in the scientific community. Tools called capillary electrophoresis and mass spectrometry have been used to study erythropoietin and the attached sugars to better develop the techniques used to study proteins and any attached sugars.
Composed of different monosaccharide units of varying atomic composition and stereochemistry, glycan structures differ from one another in their monosaccharide composition, sequence, and in the many ways by which the sequence of monosaccharides are linked together. The range of variations naturally found within glycans gives rise to microheterogeneity within an isolated sample of a glycosylated polypeptide, or “glycoprotein”. This dissertation presents and discusses the experimental and simulated data for the analysis of erythropoietin using capillary electrophoresis and mass spectrometry.
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