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http://purl.uniprot.org/citations/2474541http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2474541http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2474541http://www.w3.org/2000/01/rdf-schema#comment"The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine. In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies. This cytoskeletal component was also labeled with [3H]glucosamine in A431 cells but not in KB cells, which do not express cytokeratin 13. Its labeling was resistant to tunicamycin, suggesting that [3H]glucosamine had not been incorporated into N-linked oligosaccharides. Acid hydrolysis followed by paper and ion-exchange chromatography showed that the radioactivity in electrophoretically purified cytokeratin 13 was still present as glucosamine. Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues. The labeled carbohydrate was released by alkaline borohydride treatment and was bound by a phenylboronic acid column, indicating an O-glycosidic linkage. On Bio-Gel P-2 columns, the beta-eliminated carbohydrate co-eluted with authentic N-acetylglucosaminitol. The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)71636-0"xsd:string
http://purl.uniprot.org/citations/2474541http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)71636-0"xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/author"King I.A."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/author"King I.A."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/author"Hounsell E.F."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/author"Hounsell E.F."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/pages"14022-14028"xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/pages"14022-14028"xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/title"Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/title"Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues."xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/volume"264"xsd:string
http://purl.uniprot.org/citations/2474541http://purl.uniprot.org/core/volume"264"xsd:string
http://purl.uniprot.org/citations/2474541http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2474541
http://purl.uniprot.org/citations/2474541http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2474541
http://purl.uniprot.org/citations/2474541http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2474541
http://purl.uniprot.org/citations/2474541http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2474541
http://purl.uniprot.org/uniprot/P13646http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2474541
http://purl.uniprot.org/uniprot/P13646#attribution-1F6192F95155830926A55833B6DFD39Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/2474541