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Acrylamide—A Cysteine Alkylating Reagent for Quantitative Proteomics

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Quantitative Proteomics by Mass Spectrometry

Part of the book series: Methods in Molecular Biology ((MIMB,volume 359))

Abstract

Mass spectrometry-based relative quantification of proteins is often achieved by the labeling of two samples with isotopically light and heavy reagents. The intensities of the ions with different masses, but same chemical properties, can be reliably used for determining relative quantities. Several strategies of labeling with various weakness and strength and degrees of complexity have been described. In this chapter, we describe a simple and inexpensive protein-labeling procedure based on the use of acrylamide and deuterated acrylamide as a cysteine alkylating reagent. Gel electrophoresis is one of the most commonly used techniques for analyzing/visualizing proteins, thus, we emphasize the use of acrylamide as a labeling procedure for quantifying proteins isolated by one- and two-dimensional polyacrylamide gel electrophoresis.

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© 2007 Humana Press Inc.

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Turko, I.V., Sechi, S. (2007). Acrylamide—A Cysteine Alkylating Reagent for Quantitative Proteomics. In: Sechi, S. (eds) Quantitative Proteomics by Mass Spectrometry. Methods in Molecular Biology, vol 359. Humana Press. https://doi.org/10.1007/978-1-59745-255-7_1

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  • DOI: https://doi.org/10.1007/978-1-59745-255-7_1

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-571-2

  • Online ISBN: 978-1-59745-255-7

  • eBook Packages: Springer Protocols

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