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Briefings in Functional Genomics 2006 5(2):154-168; doi:10.1093/bfgp/ell024
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© Oxford University Press, 2006, All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Special Issue Papers

Comparison of a Salmonella typhimurium proteome defined by shotgun proteomics directly on an LTQ-FT and by proteome pre-fractionation on an LCQ-DUO

Brook L. Nunn, Scott A. Shaffer, Alexander Scherl, Byron Gallis, Manhong Wu, Samuel I. Miller and David R. Goodlett

Corresponding author. David R. Goodlett, Medicinal Chemistry Department, University of Washington, Box 335351, Seattle, WA 98195, USA. E-mail: goodlett{at}u.washington.edu

Shotgun proteomics is rapidly becoming one of the most efficient and popular tools to examine protein expression in cells. Numerous laboratories now have a wide array of low- and high-performance mass spectrometry instrumentation necessary to complete proteome-wide projects. Often these laboratories have time and financial constraints that prohibit all projects from being conducted on high-performance state-of-the-art mass spectrometers. Here, we compare shotgun proteomic results using a direct ‘lyse, digest and analyse’ approach on a high-performance mass spectrometer (i.e. the LTQ-FT) with the results from a much lower-performance instrument (i.e. the LCQ-DUO) where, for the latter, various traditional protein pre-fractionation steps and gas-phase fractionation were used to increase the proteome coverage. Our results demonstrate that shotgun proteomic analyses conducted on the lower-performance LCQ-DUO mass spectrometer could adequately characterize a PhoP constitutive strain of Salmonella typhimurium if proteome pre-fractionation steps and gas-phase fractionation were included.

Keywords: shotgun proteomics, ion trap mass spectrometer, Salmonella, linear ion trap and Fourier transform ion cyclotron resonance mass spectrometer, membrane proteome


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