{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qu Y"],"funding":["DOE-BER","EMSL intramural research projects","EMSL capability development projects","NIEHS NIH HHS","National Institute of Environmental Health Sciences of the National Institutes of Health","U.S. Department of Energy Office of Biological and Environmental Research","DOE"],"pagination":["207-215"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5175459"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["72"],"pubmed_abstract":["Protein glycosylation, an important and complex post-translational modification (PTM), is involved in various biological processes, including the receptor-ligand and cell-cell interaction, and plays a crucial role in many biological functions. However, little is known about the glycan structures of important biological complex samples, and the conventional glycan enrichment strategy (i.e., size-exclusion column [SEC] separation) prior to nuclear magnetic resonance (NMR) detection is time-consuming and tedious. In this study, we developed a glycan enrichment strategy that couples Zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC) with dialysis to enrich the glycans from the pronase E digests of RNase B, followed by NMR analysis of the glycoconjugate. Our results suggest "],"journal":["Fungal genetics and biology : FG & B"],"pubmed_title":["Structural analysis of N- and O-glycans using ZIC-HILIC/dialysis coupled to NMR detection."],"pmcid":["PMC5175459"],"funding_grant_id":["R01ES022176","R01 ES022176","DE-AC05-76RL01830"],"pubmed_authors":["Cao L","Zink EM","Deng S","Lipton MS","Pasa-Tolic L","Zhang Q","Hu JZ","Jiang Y","Feng J","Zhao R","Zhang Z","Wu S","Qu Y","Baker SE"],"additional_accession":[]},"is_claimable":false,"name":"Structural analysis of N- and O-glycans using ZIC-HILIC/dialysis coupled to NMR detection.","description":"Protein glycosylation, an important and complex post-translational modification (PTM), is involved in various biological processes, including the receptor-ligand and cell-cell interaction, and plays a crucial role in many biological functions. However, little is known about the glycan structures of important biological complex samples, and the conventional glycan enrichment strategy (i.e., size-exclusion column [SEC] separation) prior to nuclear magnetic resonance (NMR) detection is time-consuming and tedious. In this study, we developed a glycan enrichment strategy that couples Zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC) with dialysis to enrich the glycans from the pronase E digests of RNase B, followed by NMR analysis of the glycoconjugate. Our results suggest ","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Nov","modification":"2025-04-18T23:59:20.908Z","creation":"2019-03-27T02:32:12Z"},"accession":"S-EPMC5175459","cross_references":{"pubmed":["25117693"],"doi":["10.1016/j.fgb.2014.08.001"]}}