RT Journal Article
SR Electronic
T1 A Proteomic Analysis of Human Bile
JF Molecular & Cellular Proteomics
JO Mol Cell Proteomics
FD American Society for Biochemistry and Molecular Biology
SP 715
OP 728
DO 10.1074/mcp.M400015-MCP200
VO 3
IS 7
A1 Kristiansen, Troels Zakarias
A1 Bunkenborg, Jakob
A1 Gronborg, Mads
A1 Molina, Henrik
A1 Thuluvath, Paul J.
A1 Argani, Pedram
A1 Goggins, Michael G.
A1 Maitra, Anirban
A1 Pandey, Akhilesh
YR 2004
UL http://www.mcponline.org/content/3/7/715.abstract
AB 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 18O, 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. © 2004 The American Society for Biochemistry and Molecular Biology