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Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Updated: Jun 15, 2026

A Quantitative Glycomics and Proteomics Combined Purification Strategy
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Published on: March 8, 2016

Comparative glycomics using a tetraplex stable-isotope coded tag.

Michael J Bowman1, Joseph Zaia

  • 1Boston University School of Medicine, Department of Biochemistry, Center for Biomedical Mass Spectrometry, Boston, Massachusetts 02118, USA.

Analytical Chemistry
|March 17, 2010
PubMed
Summary
This summary is machine-generated.

Tetraplex stable isotope tags enable direct comparison of glycan compositions across four samples. This mass spectrometry method accurately profiles and analyzes glycan structures, including isomers, for advanced glycomics research.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Glycomics

Background:

  • Glycomics research requires precise methods for comparing complex carbohydrate structures across multiple samples.
  • Distinguishing between glycan structural isomers is crucial for understanding biological function.
  • Existing mass spectrometry techniques can be limited in direct, high-throughput comparative glycan analysis.

Purpose of the Study:

  • To demonstrate the effectiveness of tetraplex stable isotope coded tags for mass spectrometric glycomics.
  • To enable direct, quantitative comparison of glycan compositions across four distinct samples.
  • To showcase the capability of the method in distinguishing glycan structural isomers.

Main Methods:

  • Utilized tetraplex stable isotope coded tags for mass spectrometry.
  • Employed capillary-scale hydrophilic interaction chromatography with online mass spectrometry for glycan separation and detection.
  • Applied nanospray ionization and tandem mass spectrometry for structural isomer analysis.

Main Results:

  • Successfully compared glycan compositions from chondroitin sulfate proteoglycans, low molecular weight heparins, full-length heparins, and N-glycans.
  • Demonstrated the ability to discern glycan structural isomers using tandem mass spectra.
  • Generated high-quality compositional profiling data for multiple glycan classes.

Conclusions:

  • Tetraplex stable isotope tagging is a valuable tool for mass spectrometric glycomics.
  • The method facilitates direct comparison and detailed structural analysis of glycans.
  • This approach enhances the quality and efficiency of glycomics compositional profiling.