Related Experiment Video
Updated: Aug 13, 2026

20:23
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
Detection of glycosylation changes in serum and tissue proteins in cancer by lectin blotting
R E Ferguson1, D H Jackson, R Hutson
1Cancer Research UK Clinical Centre, St. James's University Hospital, Leeds L59 7TF, UK.
Advances in Experimental Medicine and Biology
|January 13, 2006
Abstract
No abstract available in PubMed .
Related Concept Videos
Western Blotting
Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
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...

