{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360004233118881024.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1021/acs.analchem.8b00714"}},{"identifier":{"@type":"URI","@value":"https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.8b00714"}},{"identifier":{"@type":"PMID","@value":"29886736"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@value":"Simultaneous Analysis of Sulfated and Phosphorylated Glycans by Serotonin-Immobilized Column Enrichment and Hydrophilic Interaction Chromatography"}],"description":[{"notation":[{"@value":"Changes in the structures and quantities of sulfated glycans play important roles in inflammatory and neurological diseases and cancer. Therefore, sulfated glycans are expected to become diagnostic markers for a variety of diseases such as Alzheimer's disease and cancer. On the other hand, structural abnormalities in the phosphorylated glycans on lysosomal enzymes cause a number of lysosomal diseases, while novel phosphorylated glycans have been found in other proteins. As with sulfated glycans, structural and quantitative changes in these phosphorylated glycans and their associations with disease are also of interest. In this article, we introduce a new method for the simultaneous analysis of sulfated and phosphorylated glycans. We first employ a serotonin-immobilized column to enrich these glycans. Glycans obtained in this manner were sequentially subjected to other analytical techniques without desalting. We employed hydrophilic interaction chromatography to distinguish the sulfate and phosphate groups of the glycans and were able to analyze sulfated and phosphorylated N-glycans expressed on thyroglobulin, ovalbumin, and myozyme. We showed that our method not only analyzes sulfated and phosphorylated glycans, but also glycans containing the GlcNAc-HPO"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1420001326214152192","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"80584185"},{"@type":"NRID","@value":"1000080584185"},{"@type":"NRID","@value":"9000307261577"},{"@type":"NRID","@value":"9000273020307"},{"@type":"NRID","@value":"9000414338921"},{"@type":"NRID","@value":"9000014182232"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/keita_yamada_page"}],"foaf:name":[{"@value":"Keita Yamada"}],"jpcoar:affiliationName":[{"@value":"The Laboratory of Toxicology, Faculty of Pharmacy, Osaka Ohtani University, 3-11-1 Nishikiori-kita, Tondabayashi, Osaka 584-8540, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233118881024","@type":"Researcher","foaf:name":[{"@value":"Haruna Kayahara"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmacy, Kindai University, 3-4-1 Kowakae, Higashi-osaka, Higashi-Osaka 577-8502, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233118881027","@type":"Researcher","foaf:name":[{"@value":"Mitsuhiro Kinoshita"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmacy, Kindai University, 3-4-1 Kowakae, Higashi-osaka, Higashi-Osaka 577-8502, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233118881025","@type":"Researcher","foaf:name":[{"@value":"Shigeo Suzuki"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmacy, Kindai University, 3-4-1 Kowakae, Higashi-osaka, Higashi-Osaka 577-8502, Japan"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00032700"},{"@type":"EISSN","@value":"15206882"}],"prism:publicationName":[{"@value":"Analytical Chemistry"}],"dc:publisher":[{"@value":"American Chemical Society 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