Skip Navigation


CIT can broadcast your seminar, conference or meeting live to a world-wide audience over the Internet as a real-time streaming video. The event can be recorded and made available for viewers to watch at their convenience as an on-demand video or a downloadable podcast. CIT can also broadcast NIH-only or HHS-only content.

Glycoproteomics Using Mass Spectrometry and Lectin Microarrays

Loading video...

239 Views  
   
Air date: Thursday, December 1, 2011, 10:00:00 AM
Time displayed is Eastern Time, Washington DC Local
Views: Total views: 239, (10 Live, 229 On-demand)
Category: Proteomics
Runtime: 01:15:58
Description: NIH Proteomics Interest Group Lecture:

Glycosylation is one of the most common forms of protein modifications. Each glycoprotein can be glycosylated at different glycosites and each glycosite may be modified by different glycans. This structural heterogeneity has complicated the study of the structure-function relationships of glycoproteins. To rapid identify and quantify the glycosylation on particular glycosites from complex biological mixtures, glycan-lectin affinity chromatography and chemical immobilization are used to isolate glycopeptides containing certain glycans, followed by mass spectrometry analysis.

We showed that upon the identification of disease-specific changes in glycosylation using lectin microarray technique, glycosites containing aberrant glycans were readily identifiable and quantifiable using the combination of lectins and mass spectrometry. The application of glycoproteomics may facilitate our understanding of how perturbed glycosylation impacts upon disease progression and could be used to discover glycosylated proteins that could serve as biomarkers or therapeutic targets to improve clinical outcomes of patients.
Debug: Show Debug
NLM Title: Glycoproteomics using mass spectrometry and lectin microarrays [electronic resource] / Hui Zhang.
Author: Zhang, Hui.
National Institutes of Health (U.S.). Proteomics Interest Group.
Publisher:
Abstract: (CIT): Glycosylation is one of the most common forms of protein modifications. Each glycoprotein can be glycosylated at different glycosites and each glycosite may be modified by different glycans. This structural heterogeneity has complicated the study of the structure-function relationships of glycoproteins. To rapid identify and quantify the glycosylation on particular glycosites from complex biological mixtures, glycan-lectin affinity chromatography and chemical immobilization are used to isolate glycopeptides containing certain glycans, followed by mass spectrometry analysis. We showed that upon the identification of disease-specific changes in glycosylation using lectin microarray technique, glycosites containing aberrant glycans were readily identifiable and quantifiable using the combination of lectins and mass spectrometry. The application of glycoproteomics may facilitate our understanding of how perturbed glycosylation impacts upon disease progression and could be used to discover glycosylated proteins that could serve as biomarkers or therapeutic targets to improve clinical outcomes of patients.
Subjects: Glycosylation
Lectins
Microarray Analysis--methods
Proteomics
Spectrum Analysis--methods
Publication Types: Lectures
Webcasts
Download: To download this event, select one of the available bitrates:
[256k]  [512k]    How to download a Videocast
Caption Text: Download Caption File
NLM Classification: QU 55.5
NLM ID: 101574498
CIT Live ID: 10816
Permanent link: https://videocast.nih.gov/launch.asp?16995