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http://purl.uniprot.org/citations/14760718http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14760718http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14760718http://www.w3.org/2000/01/rdf-schema#comment"In the last few years mass spectrometry has become the method of choice for characterization of post-translationally modified proteins. Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue. The detailed characterization of glycoproteins in complex biological samples is extremely challenging. However, information on N-glycosylation can be gained at an intermediary level. Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content. Glycosylated proteins are selected by an initial lectin chromatography step and digested with endoproteinase Lys-C. Glycosylated peptides are then selected from the digest mixture by a second lectin chromatography step. The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry. Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.org/dc/terms/identifier"doi:10.1002/pmic.200300556"xsd:string
http://purl.uniprot.org/citations/14760718http://purl.org/dc/terms/identifier"doi:10.1002/pmic.200300556"xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Bunkenborg J."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Bunkenborg J."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Pilch B.J."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Pilch B.J."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Podtelejnikov A.V."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Podtelejnikov A.V."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Wisniewski J.R."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/author"Wisniewski J.R."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/name"Proteomics"xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/name"Proteomics"xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/pages"454-465"xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/pages"454-465"xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/title"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/title"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/14760718http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/14760718http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14760718
http://purl.uniprot.org/citations/14760718http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14760718