AI Article Synopsis
- Glycosylation is a crucial post-translational modification that involves adding sugars (glycans) to proteins, impacting their function and structure.
- The analysis of glycans and glycoproteins is complex due to challenges like diverse structures and low abundance, making mass spectrometry (MS) a vital but incomplete tool for this study.
- This review highlights the importance of separation techniques, particularly liquid chromatography and capillary electrophoresis, in enhancing the analysis of glycans and glycopeptides for better structural and quantitative insights.
Article Abstract
Glycosylation is one of the most significant and abundant post-translational modifications in cells. Glycomic and glycoproteomic analyses involve the characterization of oligosaccharides (glycans) conjugated to proteins. Glycomic and glycoproteomic analysis is highly challenging because of the large diversity of structures, low abundance, site-specific heterogeneity, and poor ionization efficiency of glycans and glycopeptides in mass spectrometry (MS). MS is a key tool for characterization of glycans and glycopeptides. However, MS alone does not always provide full structural and quantitative information for many reasons, and thus MS is combined with some separation technique. This review focuses on the role of separation techniques used in glycomic and glycoproteomic analyses, liquid chromatography and capillary electrophoresis. The most important separation conditions and results are presented and discussed.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9212196 | PMC |
| http://dx.doi.org/10.1007/s00706-022-02938-4 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!