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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...

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Updated: Sep 29, 2025

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Published on: May 4, 2012

Examining Galectin Binding Specificity Using Glycan Microarrays.

Sean R Stowell^1,2, Lilian C Rodrigues³, Marcelo Dias-Baruffi³

¹Joint Program in Transfusion Medicine, Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA.

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

|March 23, 2022

Summary

This summary is machine-generated.

Glycan binding proteins (GBPs) interact with cell surface glycans. Glycan microarray platforms help define subtle structural changes impacting GBP binding specificity, particularly for the galectin family.

Keywords:

GBP–glycan interactions Galectin Glycan binding protein (GBP)Glycan microarray

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Area of Science:

Glycobiology
Protein-carbohydrate interactions
Molecular recognition

Background:

Glycan binding proteins (GBPs) regulate biological processes via cell surface glycan interactions.
Subtle glycan structural changes significantly impact GBP binding and activity, posing analytical challenges.

Purpose of the Study:

To describe methods for analyzing GBP-glycan interactions using glycan microarrays.
To investigate galectin family binding specificity and function through detailed glycan analysis.

Main Methods:

Utilized glycan microarray platforms with hundreds of structurally defined glycans.
Examined galectin-glycan binding specificity and function.

Main Results:

Glycan microarrays provide crucial insights into general GBP-glycan interactions.
Significant understanding of galectin binding specificity and biological activity was achieved.

Conclusions:

Glycan microarray technology overcomes limitations in analyzing subtle glycan structure-function relationships.
This approach enhances the study of galectin family members and their biological roles.