An evaluation of the use of two-dimensional gel electrophoresis in proteomics.
With whole genomes being sequenced almost routinely, the next logical step towards a better understanding of cellular mechanisms lies in studying the functional units of gene expression-proteins. One of the fundamental approaches in proteomics is the use of two-dimensional gel electrophoresis as a mode of separation and visualization of complex protein mixtures. Despite several limitations of the method, its ability to separate large numbers of proteins, including their post-translationally modified forms, ensures that it will continue to be popular in several well-defined areas of proteomics. In this article, we discuss the merits and drawbacks of two-dimensional gels and compare them with alternative systems such as one-dimensional gels and liquid chromatography-based separation methods. In the wake of recent advances in mass spectrometry and related areas, we outline areas where two-dimensional gels can best be utilized as the preferred separation method in proteomic strategies.
Ong
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Protein Interaction Laboratory, Center for Experimental Bioinformatics, University of Southern Denmark, Odense.
Pandey
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A
D015180:Electrophoresis, Gel, Two-Dimensional / Q000295:instrumentation / Q000379:methods; D005786:Gene Expression Regulation / Q000502:physiology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry / Q000379:methods; D020411:Oligonucleotide Array Sequence Analysis / Q000379:methods; D011506:Proteins / Q000032:analysis*; D020543:Proteome / Q000737:chemistry*; D014407:Tumor Cells, Cultured
D011506:Proteins; D020543:Proteome