Abstract
In this review we examine the current state of analytical methods in proteomics. The conventional methodology using two-dimensional electrophoresis gels and mass spectrometry is discussed, with particular reference to the advantages and shortcomings thereof. Two recently published methods which offer an alternative approach are presented and discussed, with emphasis on how they can provide information not available via two-dimensional gel electrophoresis. These two methods are the isotope-coded affinity tags approach of Gygi et al. and the two-dimensional liquid chromatography–tandem mass spectrometry approach as presented by Link et al. We conclude that both of these new techniques represent significant advances in analytical methodology for proteome analysis. Furthermore, we believe that in the future biological research will continue to be enhanced by the continuation of such developments in proteomic analytical technology.
Highlights
In this review we examine the current state of analytical methods in proteomics
This has led to the classi®cation of a new subdiscipline of protein chemistry known asproteomics', where a proteome is de®ned as the protein complement expressed by the genome of an organism or cell type [49]
In discussing analytical methods to be used in proteome analysis, consideration must be given to the fact that the number of proteins expressed at one time in a given cellular system is typically in the thousands or tens of thousands
Summary
In this review we examine the current state of analytical methods in proteomics. The conventional methodology using two-dimensional electrophoresis gels and mass spectrometry is discussed, with particular reference to the advantages and shortcomings thereof. The isolated tagged peptides are separated and analysed by microcapillary tandem mass spectrometry, which provides both identi®cation of the peptides by fragmentation in MS±MS mode and relative quantitation of labelled pairs by comparing signal intensities in MS mode.
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