A chromatographic and mass spectrometric strategy for the analysis of oligosaccharides: determination of the glycan structures in porcine thyroglobulin
| Autor: | Andrew J. Organ, Helen Birrell, Patrick Camilleri, Joanne Charlwood |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Glycan
Swine medicine.medical_treatment Neuraminidase Oligosaccharides Sialidase Thyroglobulin High-performance liquid chromatography Analytical Chemistry Capillary electrophoresis Polysaccharides medicine Animals Fucosidase Chromatography High Pressure Liquid Spectroscopy Fluorescent Dyes alpha-L-Fucosidase Chromatography biology Molecular mass Aminoacridines Chemistry Hydrolysis Organic Chemistry Electrophoresis Capillary Mass spectrometric Biochemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein |
| Zdroj: | Rapid Communications in Mass Spectrometry. 13:716-723 |
| ISSN: | 1097-0231 0951-4198 |
| DOI: | 10.1002/(sici)1097-0231(19990430)13:8<716::aid-rcm547>3.0.co;2-c |
| Popis: | Oligosaccharides released from porcine thyroglobulin were first derivatised with 2-aminoacridone (2-AMAC) and analysed by capillary electrophoresis to determine the complexity of this glycan pool. The same glycan mixture was then subjected to either a sialidase digest or a sialidase and fucosidase digest prior to derivatisation with 2-AMAC and analysis by normal phase high pressure liquid chromatography (HPLC). Comparison of the three chromatographic profiles with known standards allowed an initial identification of the glycan structures. The 2-AMAC derivatised glycans were then collected from HPLC for matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) analysis and the molecular weights of predicted structures were confirmed. This study demonstrates that a two enzyme array and subsequent MALDI-TOF analysis can be used successfully to assign the major glycans present in a complex mixture. |
| Databáze: | OpenAIRE |
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