{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Momcilovic A"],"funding":["Dutch Research Council (NWO)","European Commission"],"pagination":["4518-4526"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7252899"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["92(6)"],"pubmed_abstract":["Immunoglobulin (Ig) glycosylation is recognized for its influence on Ig turnover and effector functions. However, the large-scale profiling of Ig glycosylation in a biomedical setting is challenged by the existence of different Ig isotypes and subclasses, their varying serum concentrations, and the presence of multiple glycosylation sites per Ig. Here, a high-throughput nanoliquid chromatography (LC)- mass spectrometry (MS)-based method for simultaneous analysis of IgG and IgA glycopeptides was developed and applied on a serum sample set from 185 healthy donors. Sample preparation from minute amounts of serum was performed in 96-well plate format. Prior to trypsin digestion, IgG and IgA were enriched simultaneously, followed by a one-step denaturation, reduction, and alkylation. The obtain"],"journal":["Analytical chemistry"],"pubmed_title":["Simultaneous Immunoglobulin A and G Glycopeptide Profiling for High-Throughput Applications."],"pmcid":["PMC7252899"],"funding_grant_id":["676421","91116004","722.016.008"],"pubmed_authors":["Koeleman CAM","Hipgrave Ederveen AL","Mesker WE","Falck D","de Haan N","de Neef LA","Tollenaar R","Wuhrer M","Bondt A","de Ru A","Momcilovic A","van Veelen P","Dotz V"],"additional_accession":[]},"is_claimable":false,"name":"Simultaneous Immunoglobulin A and G Glycopeptide Profiling for High-Throughput Applications.","description":"Immunoglobulin (Ig) glycosylation is recognized for its influence on Ig turnover and effector functions. However, the large-scale profiling of Ig glycosylation in a biomedical setting is challenged by the existence of different Ig isotypes and subclasses, their varying serum concentrations, and the presence of multiple glycosylation sites per Ig. Here, a high-throughput nanoliquid chromatography (LC)- mass spectrometry (MS)-based method for simultaneous analysis of IgG and IgA glycopeptides was developed and applied on a serum sample set from 185 healthy donors. Sample preparation from minute amounts of serum was performed in 96-well plate format. Prior to trypsin digestion, IgG and IgA were enriched simultaneously, followed by a one-step denaturation, reduction, and alkylation. The obtain","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Mar","modification":"2025-04-04T09:04:50.269Z","creation":"2020-06-02T07:10:37Z"},"accession":"S-EPMC7252899","cross_references":{"pubmed":["32091889"],"doi":["10.1021/acs.analchem.9b05722"]}}