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Sheathless capillary electrophoresis-tandem mass spectrometry for top-down characterization of Pyrococcus furiosus proteins on a proteome scale

Academic Article
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Overview

authors

  • Han, X.
  • Wang, Y.
  • Aslanian, A.
  • Bern, M.
  • Lavallee-Adam, M.
  • Yates III, John

publication date

  • November 2014

journal

  • Analytical Chemistry  Journal

abstract

  • Intact protein analysis via top-down mass spectrometry (MS) provides the unique capability of fully characterizing protein isoforms and combinatorial post-translational modifications (PTMs) compared to the bottom-up MS approach. Front-end protein separation poses a challenge for analyzing complex mixtures of intact proteins on a proteomic scale. Here we applied capillary electrophoresis (CE) through a sheathless capillary electrophoresis-electrospray ionization (CESI) interface coupled to an Orbitrap Elite mass spectrometer to profile the proteome from Pyrococcus furiosus. CESI-top-down MS analysis of Pyrococcus furiosus cell lysate identified 134 proteins and 291 proteoforms with a total sample consumption of 270 ng in 120 min of total analysis time. Truncations and various PTMs were detected, including acetylation, disulfide bonds, oxidation, glycosylation, and hypusine. This is the largest scale analysis of intact proteins by CE-top-down MS to date.

subject areas

  • Archaeal Proteins
  • Electrophoresis, Capillary
  • Proteome
  • Proteomics
  • Pyrococcus furiosus
  • Tandem Mass Spectrometry
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Identity

PubMed Central ID

  • PMC4238646

International Standard Serial Number (ISSN)

  • 0003-2700

Digital Object Identifier (DOI)

  • 10.1021/ac503439n

PubMed ID

  • 25346219
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Additional Document Info

start page

  • 11006

end page

  • 11012

volume

  • 86

issue

  • 22

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