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Mass Spectrometry-Based Detection of Protein Acetylation

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Sirtuins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1077))

Abstract

Improved sample preparation techniques and increasingly sensitive mass spectrometry (MS) analysis have revolutionized the study of protein post-translational modifications (PTMs) (Rush et al., Nat Biotechnol 23:94–101, 2005). Here, we describe a general approach for immunopurification and MS-based identification of acetylated proteins in biological samples. This approach is useful to characterize changes in the acetylome in response to biological interventions (Schwer et al., Aging Cell 8:604–606, 2009).

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Acknowledgements

The authors would like to thank members of the Lombard lab for helpful discussions, and the PTMScan Service Group at Cell Signaling Technology (Matt P. Stokes, Charles L. Farnsworth, and Hongbo Gu) for their assistance in reviewing the protocol. Work in the Lombard lab is supported by NIH grants R01GM101171 and R21CA177925 (Lombard), R01HL114858 (Lukacs), DP3DK094292 (Brosius and others), and a New Scholar in Aging award from the Ellison Medical Foundation (Lombard).

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Li, Y., Silva, J.C., Skinner, M.E., Lombard, D.B. (2013). Mass Spectrometry-Based Detection of Protein Acetylation. In: Hirschey, M. (eds) Sirtuins. Methods in Molecular Biology, vol 1077. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-637-5_6

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  • DOI: https://doi.org/10.1007/978-1-62703-637-5_6

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-636-8

  • Online ISBN: 978-1-62703-637-5

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