Correlation Engine 2.0
Clear Search sequence regions


filter terms:
  • bile (5)
  • liver (1)
  • mass (2)
  • pancreas (1)
  • Sizes of these terms reflect their relevance to your search.

    One of the critical issues to warrant the success of a proteome-wide analysis is sample preparation. Efficient protein extraction in the absence of interferent material is mandatory to achieve an ample proteome coverage by mass spectrometry. The study of biological fluids is always challenging due to their specific biochemical composition. However, there is increasing interest in their characterization as it will provide proteins that may advice disease setting, state, and progression. In particular, bile is proximal to liver and pancreas, and its study is especially attractive since it might provide valuable information for the clinical management of severe diseases afflicting these organs, which are at an urgent need of new biomarkers. Though previous efforts have been made to optimize protocols to analyze bile proteome, only partial descriptions were achieved due to its complex composition, where proteins represent less than 5% of the organic components. Here we describe a new method that significantly increases the bile proteome coverage while reducing by a factor of six the amount of sample required for the proteomic analysis. © 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

    Citation

    Sergio Ciordia, Gloria Alvarez-Sola, María Rullán, Jesús M Urman, Matías A Ávila, Fernando J Corrales. Bile Processing Protocol for Improved Proteomic Analysis. Methods in molecular biology (Clifton, N.J.). 2022;2420:1-10

    Expand section icon Mesh Tags

    Expand section icon Substances


    PMID: 34905161

    View Full Text