A Proteomic Analysis of Human Bile

We have carried out a comprehensive characterization of human bile to define the bile proteome. Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry. Overall, we identified 87...

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Bibliographic Details
Published in:Molecular & cellular proteomics 2004-07, Vol.3 (7), p.715-728
Main Authors: Kristiansen, Troels Zakarias, Bunkenborg, Jakob, Gronborg, Mads, Molina, Henrik, Thuluvath, Paul J, Argani, Pedram, Goggins, Michael G, Maitra, Anirban, Pandey, Akhilesh
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bile - metabolism
Chromatography, Liquid
Electrophoresis, Polyacrylamide Gel
Humans
Isotope Labeling
Lectins - chemistry
Mass Spectrometry
Molecular Sequence Data
Proteome
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Summary:We have carried out a comprehensive characterization of human bile to define the bile proteome. Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry. Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown. A large majority of the identified proteins have not been previously described in bile. Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by 18 O, we have identified a total of 33 glycosylation sites. The strategy described in this study should be generally applicable for a detailed proteomic analysis of most body fluids. In combination with “tagging” approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
ISSN:1535-9476
1535-9484
DOI:10.1074/mcp.M400015-MCP200