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Protein Glycosylation

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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.
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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,...

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Related Experiment Video

Updated: Jun 29, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Bovine milk glycome.

N Tao¹, E J DePeters, S Freeman

¹Department of Chemistry and Biochemistry, School of Medicine, University of California, Davis 95616, USA.

Journal of Dairy Science

|October 4, 2008

Summary

Bovine milk oligosaccharides (bMO) have significant biological activities and industrial potential. This study systematically characterized bMO structures, revealing unique compositions distinct from human milk oligosaccharides.

Related Experiment Videos

Last Updated: Jun 29, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Area of Science:

Food Science
Biochemistry
Nutritional Science

Background:

Bovine milk oligosaccharides (bMO) exhibit biological activities, including pathogen inhibition and beneficial bacteria support.
bMO are recognized for potential applications in the food and pharmaceutical industries as complex carbohydrate supplements.
Current knowledge of bMO structures is limited, with no systematic characterization studies reported.

Purpose of the Study:

To systematically investigate and characterize the structures of bovine milk oligosaccharides.
To provide a comprehensive analysis of bMO composition and properties.

Main Methods:

Utilized high-performance mass spectrometry and advanced separation techniques.
Analyzed oligosaccharides present in bovine milk.

Main Results:

Identified nearly 40 distinct oligosaccharides in bovine milk.
Bovine milk oligosaccharides possess shorter oligomeric chains compared to human milk oligosaccharides.
Approximately 70% of bMO are sialylated, contributing to their anionic nature.
bMO structures are based on lactose and lactose amine cores, unlike the predominantly lactose core in human milk oligosaccharides.
Sialic acid residues include N-acetyl and N-glycolylneuraminic acid, with N-acetyl being more prevalent.

Conclusions:

Bovine milk oligosaccharides represent a complex and diverse group of compounds.
The unique structural features of bMO, including sialylation and core structures, differentiate them from human milk oligosaccharides.
Further research into bMO is warranted due to their potential biological and industrial significance.