Mass spectrometric analysis of chitooligosaccharides and their interaction with proteins

Chitooligosaccharides are composed of glycosamin and N-acetylglycisamin residues. Gel permeations chromatography is employed for the separation of oligomers, cation exchange chromatography is used for the separation of homologes and isomers. Trideuterioacetylation of the chitooligosaccharides followed by MALDI-TOF mass spectrometry allowes for the quantitation of mixtures of homologes. vMALDI LTQ multiple-stage MS is employed for quantitative sequencing of complex mixtures of heterochitooligosaccharides. Pure homologes and isomers are applied to biological assays. Chitooligosaccahrides form high-affinity non-covalent complexes with HC gp-39 (human cartilage glycoprotein of 39 kDa). The affinity of the chitooligosaccharides depends on DP, FA and the sequence of glycosamin and N-acetylglycosamin moieties. (+)nanoESI Q TOF MS/MS is used for identification of a high-affinity binding chitooligosaccharide of a non-covalent chitinase B - chitooligosaccharide complex. DADAA is identified as the heterochitoisomer binding with highest affinity and biostability to HC gp-39. Fluorescence based enzyme assays confirm the results.

Level thesis:degree_level

thesis.doctoral

Grantor dc:publisher

Universität Potsdam

Year

2008

Author dc:creator

• Bahrke, Sven

Contributors dc:contributor

• Peter, Martin Gerhard

• Chitooligosaccharide
• HPLC
• Massenspektrometrie
• Chitolektine
• Chitinase
• Chitooligosaccharides
• Mass Spectrometry
• Chitolectins

Statement dc:rights

• Keine öffentliche Lizenz: Unter Urheberrechtsschutz

Repository record source_url

https://publishup.uni-potsdam.de/frontdoor/index/index/docId/2182

OAI identifier oai:identifier

oai:kobv.de-opus4-uni-potsdam:2182