{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Marie AL"],"funding":["National Cancer Institute","NCI NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["1991-2002"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7987205"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["93(4)"],"pubmed_abstract":["We developed a highly sensitive method for profiling of N-glycans released from proteins based on capillary zone electrophoresis coupled to electrospray ionization mass spectrometry (CZE-ESI-MS) and applied the technique to glycan analysis of plasma and blood-derived isolates. The combination of dopant-enriched nitrogen (DEN)-gas introduced into the nanoelectrospray microenvironment with optimized ionization, desolvation, and CZE-MS conditions improved the detection sensitivity up to ∼100-fold, as directly compared to the conventional mode of instrument operation through peak intensity measurements. Analyses without supplemental pressure increased the resolution ∼7-fold in the separation of closely related and isobaric glycans. The developed method was evaluated for qualitative and quantitative glycan profiling of three types of blood isolates: plasma, total serum immunoglobulin G (IgG), and total plasma extracellular vesicles (EVs). The comparative glycan analysis of IgG and EV isolates and total plasma was conducted for the first time and resulted in detection of >200, >400, and >500 N-glycans for injected sample amounts equivalent to <500 nL of blood. Structural CZE-MS<sup>2</sup> analysis resulted in the identification of highly diverse glycans, assignment of α-2,6-linked sialic acids, and differentiation of positional isomers. Unmatched depth of N-glycan profiling was achieved compared to previously reported methods for the analysis of minute amounts of similar complexity blood isolates."],"journal":["Analytical chemistry"],"pubmed_title":["High-Sensitivity Glycan Profiling of Blood-Derived Immunoglobulin G, Plasma, and Extracellular Vesicle Isolates with Capillary Zone Electrophoresis-Mass Spectrometry."],"pmcid":["PMC7987205"],"funding_grant_id":["R35 GM136421","R01GM120272","R01 CA218500","R01 GM120272","R35GM136421","R01CA218500"],"pubmed_authors":["Ivanov AR","Marie AL","Jones J","Lu S","Ray S","Ghiran I"],"additional_accession":[]},"is_claimable":false,"name":"High-Sensitivity Glycan Profiling of Blood-Derived Immunoglobulin G, Plasma, and Extracellular Vesicle Isolates with Capillary Zone Electrophoresis-Mass Spectrometry.","description":"We developed a highly sensitive method for profiling of N-glycans released from proteins based on capillary zone electrophoresis coupled to electrospray ionization mass spectrometry (CZE-ESI-MS) and applied the technique to glycan analysis of plasma and blood-derived isolates. The combination of dopant-enriched nitrogen (DEN)-gas introduced into the nanoelectrospray microenvironment with optimized ionization, desolvation, and CZE-MS conditions improved the detection sensitivity up to ∼100-fold, as directly compared to the conventional mode of instrument operation through peak intensity measurements. Analyses without supplemental pressure increased the resolution ∼7-fold in the separation of closely related and isobaric glycans. The developed method was evaluated for qualitative and quantitative glycan profiling of three types of blood isolates: plasma, total serum immunoglobulin G (IgG), and total plasma extracellular vesicles (EVs). The comparative glycan analysis of IgG and EV isolates and total plasma was conducted for the first time and resulted in detection of >200, >400, and >500 N-glycans for injected sample amounts equivalent to <500 nL of blood. Structural CZE-MS<sup>2</sup> analysis resulted in the identification of highly diverse glycans, assignment of α-2,6-linked sialic acids, and differentiation of positional isomers. Unmatched depth of N-glycan profiling was achieved compared to previously reported methods for the analysis of minute amounts of similar complexity blood isolates.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Feb","modification":"2025-04-06T12:55:07.301Z","creation":"2025-04-06T12:55:07.301Z"},"accession":"S-EPMC7987205","cross_references":{"pubmed":["33433994"],"doi":["10.1021/acs.analchem.0c03102"]}}