N-glycome Analysis
N-glycome Analysis - Related Videos
11:36
Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Cited by 16 •
2016
This article presents an enhanced form of a novel bottom-up glycomics technique designed to analyze the pooled compositional profile of glycans in unfractionated biofluids through the chemical breakdown of glycans into their constituent linkage-specific monosaccharides for detection by GC-MS. Potential applications include early detection of cancer and other glycan-affective disorders.
11:38
A Quantitative Glycomics and Proteomics Combined Purification Strategy
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Cited by 18 •
2016
A high-throughput protocol was developed for combined proteomics and glycomics purification and LC-MS/MS quantification in plasma. Deamidation analysis of N-linked glycosylation motifs was specific to deglycosylated sites. Accurate quantitation of N-glycans was achieved by coupling filter aided N-glycan separation to the individuality normalization when labeling with glycan hydrazide tags strategy.
08:52
Spatial Molecular Imaging of the Glycome Using Mass Spectrometry
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Cited by 1 •
2025
This protocol details the key steps to enable rigorous and reproducible measurement of both glycogen and N-linked glycans using mass spectrometry imaging.
10:59
Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments
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Cited by 4 •
2025
This protocol details the glycomics-guided glycoproteomics method, an integrated omics technology that offers comprehensive insights into the heterogeneous glycoproteome in complex tumor microenvironments required to better understand the glycobiology of cancers.
13:06
Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry
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Cited by 6 •
2014
In order to comprehensively explore the diversity of O-linked glycans, a new procedure for in-gel reductive β-elimination, combined with permethylation and a rapid phase-partition method, is applied to the analysis of O-linked glycans directly released from glycoproteins resolved by SDS-PAGE and amenable to subsequent glycomic analysis by mass spectrometry.
FAQs
Peptide-N-glycosidase F provides the enzymatic release step that separates N-linked glycans from their glycoprotein carriers. This enables the carbohydrate structures to be examined independently rather than only as part of intact proteins. Because the released glycans can then enter chromatographic or mass-spectrometric workflows, the enzyme connects sample preparation with downstream assessment of glycan composition and structural variation.
Comparisons can focus on glycan composition, branching, and overall structural variation. These features help distinguish profiles associated with different biological states, such as development, immune responses, infection, or disease. Examining the pattern as a whole can reveal changes in glycosylation that may be difficult to recognize from measurements of protein abundance alone.
Liquid chromatography separates released glycans, while mass spectrometry supports their identification through analytical measurement of the separated material. Using these approaches together strengthens structural profiling because separation helps resolve components and mass-based analysis helps characterize their composition. Complementary glycomic methods can extend this information when a single measurement does not fully describe the observed structural diversity.
A typical workflow begins with enzymatic release of N-linked glycans using peptide-N-glycosidase F. The released material is then separated and identified by liquid chromatography, mass spectrometry, or complementary glycomic methods. Researchers compare the resulting profiles to evaluate composition, branching, and structural variation, linking analytical observations to changes in the biological sample or experimental condition.
Profile comparisons can show whether glycosylation changes between biological conditions and can highlight patterns associated with development, immune responses, infection, or disease. Such differences may support biomarker discovery and help clarify protein function. The approach therefore provides more than a structural inventory: it connects glycan variation with biological state and potential experimental or clinical relevance.
For cell-surface and secreted glycoproteins, the method helps investigate how glycosylation contributes to biological variation and protein function. In biopharmaceutical work, comparing N-glycan profiles supports development and quality control by monitoring carbohydrate-related structural features. These applications make glycomic measurements relevant both to basic biology and to the consistent characterization of biologically produced medicines.