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Direct ampholyte-free liquid-phase isoelectric peptide focusing: Application to the human serum proteome

  1. Author:
    Xiao, Z.
    Conrads, T. P.
    Lucas, D. A.
    Janini, G. M.
    Schaefer, C. F.
    Buetow, K. H.
    Issaq, H. J.
    Veenstra, T. D.

  2. Author Address

    Veenstra, TD, NCI, Lab Prote & Analyt Technol, SAIC Frederick Inc, Bldg 469,POB B, Frederick, MD 21702 USA NCI, Lab Prote & Analyt Technol, SAIC Frederick Inc, Frederick, MD 21702 USA. NCI, Ctr Bioinformat, Frederick, MD 21702 USA.
    1. Year: 2004
  2. Journal: Electrophoresis
    1. 25
    2. 1
    3. Pages: 128-133
  4. Type of Article: Article
  1. Abstract:

    In this study, we utilized a multidimensional peptide separation strategy combined with tandem mass spectrometry (MS/MS) for the identification of proteins in human serum. After enzymatically digesting serum with trypsin, the peptides were fractionated using liquid-phase isoelectric focusing (IEF) in a novel ampholyte-free format. Twenty IEF fractions were collected and analyzed by reversed-phase microcapillary liquid chromatography (muLC)-MS/MS. Bioinformatic analysis of the raw MS/MS spectra resulted in the identification of 844 unique peptides, corresponding to 437 proteins. This study demonstrates the efficacy of ampholyte-free peptide autofocusing, which alleviates peptide losses in ampholyte removal strategies. The results show that the separation strategy is effective for high-throughput characterization of proteins from complex proteomic mixtures

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