Publikationstyp: Konferenz: Sonstiges
Art der Begutachtung: Keine Angabe
Titel: Mass spectrometry-based glycan analysis of the glycoprotein ricin
Autor/-in: Thurnheer, Anina
Josuran, Roland
Müller, Christian
Avondet, Marc-André
Zaborosch, Christiane
Angaben zur Konferenz: Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015
Erscheinungsdatum: 2015
Sprache: Englisch
Schlagwörter: Mass spectrometry; Glycan analysis
Fachgebiet (DDC): 572: Biochemie
Zusammenfassung: Ricin is a potent toxin from the plant Ricinus communis which is included on list 1 of the Chemical Weapons Convention because of its high toxicity and easy availability. Ricin is present as a 59 kDa glycoprotein in the seeds of Ricinus communis and consists of two disulphide-linked subunits. N-glycan species of ricin were identified by enzymatic cleavage from the protein part, separation of the glycan species by porous graphitized carbon chromatography (PGCC) and detection with an electrospray ionization quadrupole time‐of-flight mass spectrometer (ESI‐Q‐TOF‐MS). Glycosylation sites in the protein were identified by capillary electrophoresis separation of proteolytically digested glycopeptides coupled to a mass spectrometer (CE‐MS). In addition, a CE method was established for the analysis of the monosaccharide composition of glycans with detection by means of LED‐induced fluorescence (CE-LEDIF). Ricin was shown to contain high‐mannose type glycans with additional monosaccharides, such as xylose, and different linkages of monosaccharide building locks compared to animal glycoproteins. Ten different high-mannose glycan species of ricin were identified using PGCC‐MS analysis. Linkages of the monosaccharide building blocks of the glycans were further characterized by exoglycosidase digestion with α(1‐2)‐mannosidase and α(1‐6)‐mannosidase.
Weitere Angaben: Oral Presentation
URI: https://digitalcollection.zhaw.ch/handle/11475/15269
Volltext Version: Publizierte Version
Lizenz (gemäss Verlagsvertrag): Keine Angabe
Departement: Life Sciences und Facility Management
Organisationseinheit: Institut für Chemie und Biotechnologie (ICBT)
Publiziert im Rahmen des ZHAW-Projekts: Aufbau der Kompetenz und Machbarkeitsstudie zur Analytik pflanzlicher Glykanstrukturen und in Pflanzenzellen hergestellter Glykoproteine
Enthalten in den Sammlungen:Publikationen Life Sciences und Facility Management

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Thurnheer, A., Josuran, R., Müller, C., Avondet, M.-A., & Zaborosch, C. (2015). Mass spectrometry-based glycan analysis of the glycoprotein ricin. Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015.
Thurnheer, A. et al. (2015) ‘Mass spectrometry-based glycan analysis of the glycoprotein ricin’, in Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015.
A. Thurnheer, R. Josuran, C. Müller, M.-A. Avondet, and C. Zaborosch, “Mass spectrometry-based glycan analysis of the glycoprotein ricin,” in Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015, 2015.
THURNHEER, Anina, Roland JOSURAN, Christian MÜLLER, Marc-André AVONDET und Christiane ZABOROSCH, 2015. Mass spectrometry-based glycan analysis of the glycoprotein ricin. In: Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015. Conference presentation. 2015
Thurnheer, Anina, Roland Josuran, Christian Müller, Marc-André Avondet, and Christiane Zaborosch. 2015. “Mass Spectrometry-Based Glycan Analysis of the Glycoprotein Ricin.” Conference presentation. In Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015.
Thurnheer, Anina, et al. “Mass Spectrometry-Based Glycan Analysis of the Glycoprotein Ricin.” Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015, 2015.


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