25 research outputs found
Structural analysis of the glycoprotein allergen Hev b 4 from natural rubber latex by mass spectrometry
6 page(s
The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris
9 page(s
Sialic acid concentrations in plants are in the range of inadvertent contamination
6 page(s
Comparative characterisation of recombinant invertebrate and vertebrate peptide O-Xylosyltransferases
12 page(s
Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
Two LC-ESI-MS methods for the analysis of antibody glycosylation are presented. In the first approach, tryptic glycopeptides are separated by RP chromatography and analyzed by ESI-MS. This "glycopeptide strategy" allows a protein- and subclass-specific quantitation of both neutral and sialylated glycan structures. Additional information about under- or deglycosylation and the protein backbone, e.g., termini, can be extracted from the same data. In the second LC-ESI-MS method, released oligosaccharides are separated on porous graphitic carbon (PGC). A complete structural assignment of neutral and sialylated oligosaccharides occurring on antibodies is thereby achieved in one chromatographic run. The two methods were applied to polyclonal human IgG, to commercial mAb expressed in CHO cells (Rituximab, Xolair, and Herceptin), in SP2/0 (Erbitux and Remicade) or NS0 cells (Zenapax) and the anti-HIV antibody 4E10 produced either in CHO cells or in a human cell line. Both methods require comparably little sample preparation and can be applied to SDS-PAGE bands. They both outperform non-MS methods in terms of reliability of peak assignment and MALDI-MS of underivatized glycans with regard to the recording of sialylated structures. Regarding fast and yet detailed structural assignment, LC-MS on graphitic carbon supersedes all other current methods.14 page(s
Identification by immunoblot of venom glycoproteins displaying immunoglobulin E-binding N-glycans as cross-reactive allergens in honeybee and yellow jacket venom
10 page(s
Distal side tryptophan, tyrosine and methionine in catalase-peroxidases are covalently linked in solution
6 page(s
Molecular cloning and characterization of a plant ?1,3/4-fucosidase based on sequence tags from almond fucosidase I
8 page(s
Comprehensive glyco-proteomic analysis of human ?1-antitrypsin and its charge isoforms
12 page(s