{"entity": "publication", "iuid": "9b74e97475674662aec42e2c29afbbcc", "timestamp": "2026-08-13T00:10:16.153Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/9b74e97475674662aec42e2c29afbbcc.json"}, "display": {"href": "https://publications.scilifelab.se/publication/9b74e97475674662aec42e2c29afbbcc"}}, "title": "High-Throughput Analysis of the Plasma N-Glycome by UHPLC.", "authors": [{"family": "Adamczyk", "given": "Barbara", "initials": "B"}, {"family": "St\u00f6ckmann", "given": "Henning", "initials": "H"}, {"family": "O'Flaherty", "given": "R\u00f3is\u00edn", "initials": "R"}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG"}, {"family": "Rudd", "given": "Pauline M", "initials": "PM"}], "type": "journal article", "published": "2016-10-16", "journal": {"title": "Methods Mol. Biol.", "issn": "1940-6029", "volume": "1503", "issue": null, "pages": "97-108", "issn-l": "1064-3745"}, "abstract": "The understanding of glycosylation alterations in health and disease has evolved significantly and glycans are considered to be relevant biomarker candidates. High-throughput analytical technologies capable of generating high-quality, large-scale glycoprofiling data are in high demand. Here, we describe an automated sample preparation workflow and analysis of N-linked glycans from plasma samples using hydrophilic interaction liquid chromatography with fluorescence detection on an ultrahigh-performance liquid chromatography (UHPLC) instrument. Samples are prepared in 96-well plates and the workflow features rapid glycoprotein denaturation, enzymatic glycan release, glycan purification on solid-supported hydrazide, fluorescent labeling, and post-labeling cleanup with solid-phase extraction. The development of a novel approach for plasma N-glycan analysis and its implementation on a robotic platform significantly reduces the time required for sample preparation and minimizes technical variation. It is anticipated that the developed method will contribute to expanding high-throughput capabilities to analyze protein glycosylation.", "doi": "10.1007/978-1-4939-6493-2_8", "pmid": "27743361", "labels": {"Glycoproteomics and MS Proteomics": "Technology development"}, "xrefs": [], "notes": [], "created": "2020-01-30T16:24:15.512Z", "modified": "2024-01-16T13:46:32.932Z"}