Publication type: | Conference other |
Type of review: | Not specified |
Title: | Mass spectrometry-based glycan analysis of the glycoprotein ricin |
Authors: | Thurnheer, Anina Josuran, Roland Müller, Christian Avondet, Marc-André Zaborosch, Christiane |
Conference details: | Chanalysis - Meeting of the Division Analytical Sciences of the Swiss Chemical Society (SCG/DAS), Beatenberg, 10 April 2015 |
Issue Date: | 2015 |
Language: | English |
Subjects: | Mass spectrometry; Glycan analysis |
Subject (DDC): | 572: Biochemistry |
Abstract: | 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. |
Further description: | Oral Presentation |
URI: | https://digitalcollection.zhaw.ch/handle/11475/15269 |
Fulltext version: | Published version |
License (according to publishing contract): | Not specified |
Departement: | Life Sciences and Facility Management |
Organisational Unit: | Institute of Chemistry and Biotechnology (ICBT) |
Published as part of the ZHAW project: | Aufbau der Kompetenz und Machbarkeitsstudie zur Analytik pflanzlicher Glykanstrukturen und in Pflanzenzellen hergestellter Glykoproteine |
Appears in collections: | 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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