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
License (according to publishing contract) : Not specified
Type of review: Not specified
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
Departement: Life Sciences and Facility Management
Organisational Unit: Institute of Chemistry and Biotechnology (ICBT)
Publication type: Conference Other
URI: https://digitalcollection.zhaw.ch/handle/11475/15269
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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