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Improving the glycoproteomic workflow for the analysis of N-linked glycans by CE/LIF
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SYSNO ASEP 0584031 Document Type A - Abstract R&D Document Type The record was not marked in the RIV R&D Document Type Není vybrán druh dokumentu Title Improving the glycoproteomic workflow for the analysis of N-linked glycans by CE/LIF Author(s) Smolková, Denisa (UIACH-O)
Bobálová, Janette (UIACH-O) RID, ORCID
Strouhalová, Dana (UIACH-O)
Čmelík, Richard (UIACH-O) RID
Lavická, Jana (UIACH-O) ORCID, RIDNumber of authors 5 Source Title CE Forum 2024. - Aalen : Aalen University, 2024
S. 18-18Number of pages 1 s. Publication form Online - E Action CE Forum 2024 Event date 28.02.2024 - 29.02.2024 VEvent location Aalen Country DE - Germany Event type EUR Language eng - English Country DE - Germany Keywords N-linked glycans ; CE/LIF Subject RIV CB - Analytical Chemistry, Separation OECD category Analytical chemistry R&D Projects GA22-00236S GA ČR - Czech Science Foundation (CSF) Institutional support UIACH-O - RVO:68081715 Annotation Structural and quantitative changes in N-linked glycans are involved in several human disorders. High-throughput profiling of N-glycans is a key step to elucidate the functions of glycans in biological processes and disease development and to discover new diagnostic biomarkers. In this work, we have optimized a workflow for the analysis of N-linked glycans by CE/LIF. Glycoproteomic protocols differing in enzymatic or digestion procedures (alkylation, gel/solution treatment, purification step, etc.) were evaluated to achieve highly sensitive detection. The released glycans were derivatized with Cascade Blue hydrazide (8-(2-hydrazino-2-oxoethoxy)pyrene-1,3,6-trisulfonic acid trisodium salt, CBH) as a more reactive analogue of 8-aminopyrene-1,3,6-trisulfonic acid trisodium salt (APTS) followed by CE/LIF analysis. Workplace Institute of Analytical Chemistry Contact Iveta Drobníková, drobnikova@iach.cz, Tel.: 532 290 234 Year of Publishing 2025 Electronic address https://hdl.handle.net/11104/0352035
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