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Two-Dimensional Polyarcylamide Gel Electrophoresis for Proteome Analyses

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 244))

Abstract

The term “proteome” can be defined, in an analogous manner to the term “genome,” as the complement of the proteins in a biological system. Undertaking a proteomic analysis enables the identification and quantitation of proteins on a proteomewide scale, thereby allowing comparisons between different proteomes. The current methodology of choice for proteome analysis is based on protein separation by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). 2-D PAGE technology, by virtue of differences in protein charge and molecular mass, allows the resolution of many thousands of proteins at the same time (see Fig. 1).

Typical two-dimensional sodium dodecyl sulfate-polyacrylamide gel. A total cellular protein extract from Saccharomyces cerevisiae was separated using pH 4–7 immobilized pH gradient (IPG) strips in the first dimension and 12% SDS-PAGE in the second dimension. Proteins were visualized by silver staining.

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© 2004 Humana Press Inc., Totowa, NJ

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Jones, N.A. (2004). Two-Dimensional Polyarcylamide Gel Electrophoresis for Proteome Analyses. In: Cutler, P. (eds) Protein Purification Protocols. Methods in Molecular Biology, vol 244. Humana Press. https://doi.org/10.1385/1-59259-655-X:353

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  • DOI: https://doi.org/10.1385/1-59259-655-X:353

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-067-0

  • Online ISBN: 978-1-59259-655-3

  • eBook Packages: Springer Protocols

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