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Depletion and fractionation technologies in plasma proteomic analysis
Sun W Tam1, John Pirro, Douglas Hinerfeld
1Charles River Proteomic Services, 57 Union Street, Worcester, MA 01608, USA. sunny.tam@dds.criver.com
Expert Review of Proteomics
|June 22, 2005
Summary
This review covers plasma protein depletion and subfractionation techniques to improve the analysis of low-abundance proteins. These methods enhance the identification of diagnostic markers and potential drug targets from plasma samples.
Area of Science:
- Proteomics
- Biochemistry
- Analytical Chemistry
Background:
- Plasma proteomics is crucial for biomarker discovery.
- Highly abundant proteins (e.g., albumin, IgG) mask low-abundance proteins.
- Current methods require enrichment of low-abundance proteins for detailed analysis.
Purpose of the Study:
- To review traditional and current technologies for plasma protein depletion and subfractionation.
- To highlight the benefits of enriching low-abundance proteins for comprehensive analysis.
- To discuss the application of these techniques in identifying diagnostic markers and drug targets.
Main Methods:
- Protein depletion techniques to remove abundant proteins like albumin and IgG.
- Subfractionation of depleted plasma based on isoelectric point.
- Analysis of protein fractions using 2D gel electrophoresis and mass spectrometry.
Main Results:
- Depletion enriches low-abundant proteins, facilitating their study.
- Subfractionation creates discrete protein pools for detailed analysis.
- These methods improve the identification of low-abundance proteins and cleaved peptides.
Conclusions:
- Plasma protein depletion and subfractionation are essential for advancing proteomics.
- These techniques enhance the discovery of novel plasma diagnostic markers.
- Improved analytical strategies can revitalize the development of plasma-based diagnostic tests.