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Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis

Academic Article
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Overview

authors

  • Cantin, G. T.
  • Yi, W.
  • Lu, B. W.
  • Park, S. K.
  • Xu, T.
  • Lee, Jiing-Dwan
  • Yates III, John

publication date

  • March 2008

journal

  • Journal of Proteome Research  Journal

abstract

  • Immobilized metal affinity chromatography (IMAC) is a common strategy used for the enrichment of phosphopeptides from digested protein mixtures. However, this strategy by itself is inefficient when analyzing complex protein mixtures. Here, we assess the effectiveness of using protein-based IMAC as a pre-enrichment step prior to peptide-based IMAC. Ultimately, we couple the two IMAC-based enrichments and MudPIT in a quantitative phosphoproteomic analysis of the epidermal growth factor pathway in mammalian cells identifying 4470 unique phosphopeptides containing 4729 phosphorylation sites.

subject areas

  • Chromatography, Affinity
  • HeLa Cells
  • Humans
  • Phosphoproteins
  • Proteome
  • Tandem Mass Spectrometry
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Research

keywords

  • EGF
  • IMAC
  • SILAC
  • phosphoproteome
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Identity

International Standard Serial Number (ISSN)

  • 1535-3893

Digital Object Identifier (DOI)

  • 10.1021/pr0705441

PubMed ID

  • 18220336
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Additional Document Info

start page

  • 1346

end page

  • 1351

volume

  • 7

issue

  • 3

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