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Molecular & Cellular Proteomics 3:715-728, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

A Proteomic Analysis of Human Bile^*

Troels Zakarias Kristiansen^,, Jakob Bunkenborg^,, Mads Gronborg^,, Henrik Molina^,, Paul J. Thuluvath^¶, Pedram Argani^||, Michael G. Goggins^||, Anirban Maitra^|| and Akhilesh Pandey^,**

From the McKusick-Nathans Institute of Genetic Medicine and Department of Biological Chemistry, Johns Hopkins University, Baltimore, MD 21205; Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, Odense M, Denmark; and Departments of ^¶ Gastroenterology and ^|| Pathology, Johns Hopkins University, Baltimore, MD 21287

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.

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