Related Experiment Video
Updated: Aug 12, 2026

10:17
Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
Published on: April 28, 2010
Glycosylation analysis of gel-separated proteins
Proteomics
|October 30, 2001
Summary
This review highlights the underrepresentation of protein glycosylation analysis in proteomics due to its complexity. It discusses current technologies for analyzing protein glycosylation and their application in proteomics research.
Area of Science:
- Proteomics
- Glycobiology
- Biochemistry
Background:
- Post-translational modifications (PTMs) are crucial for protein function and cellular communication.
- Glycosylation, a complex PTM, is often overlooked in proteomics research.
- Advanced analytical techniques are needed for detailed characterization of protein modifications.
Observation:
- Proteomics typically focuses on protein identification rather than detailed modification analysis.
- The analytical complexity of glycan analysis hinders its integration into standard proteomics workflows.
- Current technologies for global and site-specific glycosylation analysis of gel-separated proteins are available.
Findings:
- This review critically examines the technological status of glycosylation analysis in proteomics.
- It assesses the utility of current methods for studying protein glycosylation.
- The discussion focuses on applying these technologies to enhance proteomic studies.
Implications:
- Improved glycosylation analysis can reveal new insights into protein function and regulation.
- Integrating glycosylation analysis into proteomics workflows will advance understanding of cellular processes.
- This can lead to novel biomarkers and therapeutic targets in various diseases.
Related Concept Videos
Protein Glycosylation
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
DNA Agarose Gel Electrophoresis
Agarose gel electrophoresis is a laboratory technique commonly used to separate DNA fragments by size. However, it can also be used to isolate and purify DNA fragments using a gel extraction protocol.
Gel extraction follows five major steps: running gel electrophoresis to separate fragments, isolating the individual bands, extracting DNA from those bands, and removing the dye and salts from the extracted mixture to obtain pure DNA.
In cloning experiments, both the insert and vector DNA...
Gel extraction follows five major steps: running gel electrophoresis to separate fragments, isolating the individual bands, extracting DNA from those bands, and removing the dye and salts from the extracted mixture to obtain pure DNA.
In cloning experiments, both the insert and vector DNA...
SDS-PAGE
Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Two-dimensional Gel Electrophoresis
Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...

