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Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

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Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
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Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Mass Spectrometry-Based Quantitative O-GlcNAcomic Analysis.

Junfeng Ma1, Gerald W Hart2

  • 1Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD, 21205-2185, USA.

Methods in Molecular Biology (Clifton, N.J.)
|February 13, 2016
PubMed
Summary
This summary is machine-generated.

O-linked β-D-N-acetylglucosamine modification (O-GlcNAcylation) is vital for cellular processes. This study presents a new method for identifying and quantifying O-GlcNAc proteins and peptides in complex biological samples.

Keywords:
Chemoenzymatic labelingElectron transfer dissociation (ETD)GalT1 labelingO-GlcNAcomeO-GlcNAcylationPhotocleavageQuantitative mass spectrometrySILACSite mapping

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Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Signaling
  • Proteomics

Background:

  • O-linked β-D-N-acetylglucosamine modification (O-GlcNAcylation) is a dynamic post-translational modification (PTM) crucial for numerous cellular functions and implicated in various physiological and pathological conditions.
  • The "O-GlcNAcome" encompasses all O-GlcNAcylated proteins, their specific modification sites, and the dynamic nature of these modifications in response to cellular stimuli.
  • Comprehensive O-GlcNAcomic analysis has historically presented significant challenges in the field of proteomics.

Purpose of the Study:

  • To introduce and detail a novel methodology for the comprehensive analysis of the O-GlcNAcome.
  • To enable the identification and quantification of O-GlcNAc proteins and peptides from intricate biological matrices.
  • To overcome previous limitations in O-GlcNAcomic profiling.

Main Methods:

  • Description of a recently developed analytical approach for O-GlcNAcomic profiling.
  • Utilizing advanced techniques for the identification of O-GlcNAc-modified peptides within complex proteomic samples.
  • Implementation of quantitative strategies to measure the abundance of O-GlcNAc proteins and peptides.

Main Results:

  • Successful identification of numerous O-GlcNAc proteins and peptides using the novel approach.
  • Demonstration of the method's capability to quantify O-GlcNAc modifications in complex biological samples.
  • Validation of the approach for robust O-GlcNAcomic analysis.

Conclusions:

  • The presented approach offers a significant advancement for O-GlcNAcomic studies.
  • This methodology facilitates a deeper understanding of the roles of O-GlcNAcylation in cellular physiology and disease.
  • The developed technique provides a powerful tool for future research into the O-GlcNAcome.