By D.F. Hochstrasser, R. D. Appel, K. L. Williams, Marc R. Wilkins, Keith L. Williams, Ron D. Appel, Denis F. Hochstrasser
Contemporary advances in two-dimensional electrophoresis, protein microanalysis and bioinformatics have made the large-scale, systematic research of proteins and their post-translational adjustments from any tissue or organism attainable. This method has bought the identify "Proteome Research", and will be regarded as the center of useful genomics. the result of proteome research exhibit which genes are expressed, how the protein items are transformed, and the way they have interaction, making proteome examine of primary significance for the biologist, clinician, and pharmaceutical undefined.
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Extra resources for Proteome Research: New Frontiers in Functional Genomics
Sample text
2 An overview of protein identification strategies Given that the best way of currently separating and visualising a proteome is through 2-D gel electrophoresis, the challenge that then arises is how the hundreds to thousands of proteins of a proteome can be identified with a minimum of effort and in a cost- and time-effective manner. Here we will not consider the more traditional protein identification methods such as immunoblotting (see Sect. 6), chemical sequencing of internal peptides, comigration analysis of known and unknown proteins, or overexpression of homologous genes of interest in an organism under study.
During SYPRO Orange and Red staining the proteins are not fixed in the gel, so blotting to membranes can be done after staining. However, correct staining requires that the proteins are coated in SDS, so the drawbacks that affect silver staining are also inherent to this type of stain. SDS binding to proteins is affected by amino acid composition and in particular, post-translational modifications such as glycosylation. Therefore SYPRO dye binding is not uniform for all the protein species on a 2-D PAGE gel.
An alternative approach to quantitation is to use staining only as a means to localise spots after 2-D PAGE and blotting to PVDF. Wilkins et al. (1996) proposed the use of high throughput rapid amino acid analysis for protein quantitation on PVDF blots. Amino acid analysis measures the protein composition and thus can determine the quantity of a particular protein in molar or gram terms. 7 Future directions for 2-D PAGE In the last twenty-five years many technical advances have been implemented to make 2-D PAGE a very powerful method for the separation and purification of complex protein mixtures.