Identification of bisecting N-glycans in tandem mass spectra using a procainamide labeling approach for in-depth N-glycan profiling of biological samples
dc.contributor.author | Kayili, Haci Mehmet | |
dc.date.accessioned | 2024-09-29T15:57:21Z | |
dc.date.available | 2024-09-29T15:57:21Z | |
dc.date.issued | 2020 | |
dc.department | Karabük Üniversitesi | en_US |
dc.description.abstract | Bisecting N-glycan structures, which are commonly observed in glycoproteins, regulate many important functions in organisms. Tandem mass spectrometry is the most frequently utilized approach for the identification of bisecting N-glycan structures. However, it can be difficult to obtain fragments to recognize bisecting N-glycans based on the analysis performed, i.e., by using hydrophilic interaction liquid chromatography equipped with a fluorescence detector and a quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). The misinterpretation of bisecting N-glycans for other types of N-glycans is possible. Therefore, a method is needed to specifically recognize bisecting N-glycan structures. This report introduces a facile strategy based on tandem mass spectrometry to identify bisecting N-glycans by using a procainamide labeling approach that increases both the mass spectrometric and the fluorescence detection sensitivity of the N-glycans. In this strategy, the precursor ions belonging to bisecting N-glycans were used by extracting the detected diagnostic fragment ions, including proc-H1N3 (m/z 1009.481+) and proc-H1N3F1 (m/z 1155.5391, in the corresponding tandem mass spectra. Subsequently, the structures of the bisecting N-glycans were confirmed. The presented strategy was applied to human IgG glycoprotein and human plasma glycoproteome. Finally, stepping energy-collision induced dissociation (SE-CID) was applied to validate the diagnostic fragments. This approach enables bisecting N-glycans to be verified and can be used for further mass spectrometry-based glycan analysis of biological samples. (C) 2020 Elsevier B.V. All rights reserved. | en_US |
dc.identifier.doi | 10.1016/j.ijms.2020.116412 | |
dc.identifier.issn | 1387-3806 | |
dc.identifier.issn | 1873-2798 | |
dc.identifier.scopus | 2-s2.0-85090193255 | en_US |
dc.identifier.scopusquality | Q3 | en_US |
dc.identifier.uri | https://doi.org/10.1016/j.ijms.2020.116412 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14619/4761 | |
dc.identifier.volume | 457 | en_US |
dc.identifier.wos | WOS:000579445000010 | en_US |
dc.identifier.wosquality | Q3 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartof | International Journal of Mass Spectrometry | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Bisecting N-Glycans | en_US |
dc.subject | Tandem mass spectrometry | en_US |
dc.subject | Procainamide labeling | en_US |
dc.subject | Glycosylation | en_US |
dc.title | Identification of bisecting N-glycans in tandem mass spectra using a procainamide labeling approach for in-depth N-glycan profiling of biological samples | en_US |
dc.type | Article | en_US |