In-depth Profiling of N-glycans Isolated from Ostrich Egg White and Yolk Glycoproteomes by HPLC-HILIC-FLD-MS/MS
dc.contributor.author | Kayili, H.M. | |
dc.date.accessioned | 2024-09-29T16:16:15Z | |
dc.date.available | 2024-09-29T16:16:15Z | |
dc.date.issued | 2021 | |
dc.department | Karabük Üniversitesi | en_US |
dc.description.abstract | Protein glycosylation is an essential post-translational modification and modulates critical cellular events. It is known that N-glycosylated proteins from egg white and yolk are played crucial roles in various cellular pathways. Characterization of N-glycan structures of glycoproteomes is required to understand these functions. Therefore, this study is aimed to characterize the N-glycan profiles of ostrich egg white and yolk glycoproteomes. In the study, N-glycans were released from ostrich egg white and yolk glycoproteomes by an enzymatical process and labeled with a procainamide tag. Samples were analyzed by HPLC-HILIC-FLD-MS/MS (high-performance hydrophilic interaction liquid chromatography with fluorescence and tandem mass spectrometric detection). The number of detected N-glycans obtained from ostrich egg white and yolk glycoproteomes was found to be 39 and 36, respectively. It was determined that N-glycans of ostrich egg white glycoproteome were highly galactosylated (96.64%). In addition, bisecting N-glycans were abundant in ostrich egg white glycoproteome (91.72%) compared to ostrich egg yolk glycoproteome (6.74%). The abundance of high-mannose N-glycans was dramatically higher in the ostrich egg yolk glycoproteome (55.84%) than the ostrich egg yolk glycoproteome (2.67%). The fucosylation ratio of N-glycans belonging to ostrich egg white and yolk glycoproteomes was detected to be 4.52% and 0.95%, respectively. The obtained data showed that N-glycan profiles of ostrich egg white and yolk glycoproteomes differed significantly. © 2021, Adiyaman University. All rights reserved. | en_US |
dc.identifier.doi | 10.37094/adyujsci.934336 | |
dc.identifier.endpage | 204 | en_US |
dc.identifier.issn | 2147-1630 | |
dc.identifier.issue | 1 | en_US |
dc.identifier.scopus | 2-s2.0-85159796266 | en_US |
dc.identifier.scopusquality | N/A | en_US |
dc.identifier.startpage | 191 | en_US |
dc.identifier.trdizinid | 436423 | en_US |
dc.identifier.uri | https://doi.org/10.37094/adyujsci.934336 | |
dc.identifier.uri | https://search.trdizin.gov.tr/tr/yayin/detay/436423 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14619/8965 | |
dc.identifier.volume | 11 | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.indekslendigikaynak | TR-Dizin | en_US |
dc.language.iso | en | en_US |
dc.publisher | Adiyaman University | en_US |
dc.relation.ispartof | Adiyaman University Journal of Science | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.subject | Glycomics | en_US |
dc.subject | Glycosylation | en_US |
dc.subject | HPLC | en_US |
dc.subject | Mass spectrometry | en_US |
dc.subject | Ostrich egg white | en_US |
dc.subject | Ostrich egg yolk | en_US |
dc.title | In-depth Profiling of N-glycans Isolated from Ostrich Egg White and Yolk Glycoproteomes by HPLC-HILIC-FLD-MS/MS | en_US |
dc.title.alternative | Devekuşu Yumurta Akı ve Sarısı Glikoproteomlarından İzole Edilmiş N-glikanların HPLC-HILIC-FLD-MS/MS ile Derinlemesine Profillenmesi | en_US |
dc.type | Article | en_US |