A proteomic analysis of human bile.

Article Details


Kristiansen TZ, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P, Goggins MG, Maitra A, Pandey A

A proteomic analysis of human bile.

Mol Cell Proteomics. 2004 Jul;3(7):715-28. Epub 2004 Apr 14.

PubMed ID
15084671 [ View in PubMed

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.

DrugBank Data that Cites this Article

NameUniProt ID
Gamma-glutamyltranspeptidase 1P19440Details
Alpha-1-acid glycoprotein 1P02763Details
Angiotensin-converting enzyme 2Q9BYF1Details
Aminopeptidase NP15144Details
Neutrophil gelatinase-associated lipocalinP80188Details
Beta-2-glycoprotein 1P02749Details
Alpha-1-acid glycoprotein 2P19652Details
Ig gamma-2 chain C regionP01859Details
Ig alpha-2 chain C regionP01877Details
Ig alpha-1 chain C regionP01876Details
Immunoglobulin J chainP01591Details