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Oligosaccharide Assembly

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...

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

Protein Glycosylation

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...

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Related Experiment Video

Updated: Jun 12, 2025

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Published on: November 20, 2014

Exploring the O-glycomic Degradome Using Natural Mucin Libraries.

Marthe Tofthagen¹, Chunsheng Jin², Piyush Patel^3,4

¹Faculty of Health Sciences, Department of Life Sciences and Health, Oslo Metropolitan University, Oslo, Norway.

Methods in Molecular Biology (Clifton, N.J.)

|June 11, 2025

Summary

This summary is machine-generated.

This study presents a method to analyze how gut bacteria break down intestinal mucins. Understanding mucin oligosaccharide degradation is key to studying the gut microbiome and its role in health and disease.

Keywords:

Chromatography Dot blotting Exoglycosidase assay LC-MS Mass spectrometry Microbiota Mucin degradation Mucins O-glycosylation

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Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

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Last Updated: Jun 12, 2025

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Published on: November 20, 2014

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Published on: June 14, 2016

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Published on: September 21, 2012

Area of Science:

Microbiology
Glycobiology
Gastroenterology

Background:

Intestinal mucins and gut microbiota interactions are vital for digestion, metabolism, and immunity.
Studying the degradation of mucin oligosaccharides by commensal bacteria is essential for understanding gut health.

Purpose of the Study:

To describe a workflow for studying the degradation of mucin oligosaccharides from isolated mucins.
To identify intestinal oligosaccharides degraded by commensal flora.
To expand the understanding of the intestinal glycomic degradome.

Main Methods:

Purification of mucins from intestinal tissues.
Treatment of mucins with fecal glycosidases from commensal bacteria.
Release, characterization, and quantification of remaining oligosaccharides using LC-MS².

Main Results:

Identification of specific intestinal oligosaccharides degraded by commensal bacteria.
Characterization of the glycan structures involved in mucus degradation.
Demonstration of a workflow using relevant glyco-substrates.

Conclusions:

The workflow enables the investigation of mucus degradation patterns by gut microbiota.
This approach is crucial for identifying pathological conditions linked to intestinal dysbiosis.
It addresses the lack of commercially available characterized glycans for intestinal studies.