Contribution of solid-phase hexapeptide ligand libraries to the repertoire of human bile proteins
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- 作者：L. Guerrier ; S. Claverol ; L. Finzi ; F. Paye ; F. Fortis ; E. Boschetti ; C. Housset
- 关键词：Bile proteins ; Chromatography ; Proteomics ; Peptide ligands ; Mass spectrometry
- 刊名：Journal of Chromatography A
- 出版年：2007
- 出版时间：28 December 2007
- 年：2007
- 卷：1176
- 期：1-2
- 页码：192-205
- 全文大小：3760 K
文摘
Proteins in bile may have important physiological functions and serve as disease biomarkers. Here, the protein composition of human gallbladder bile was analyzed using a recently described chromatography-like technology capable to enhance the signal of low-abundance species. First, proteins present in bile fluid were treated with immobilized peptide ligand libraries to concentrate dilute and very dilute species while concomitantly diluting the high-abundance proteins. The analysis of resulting protein mixture was then performed using LC–MS/MS after having classically separated proteins by a mini preparative gel electrophoresis. Overall 222 gene products were found; 143 of them were not reported before in proteomics studies. Ligand libraries by themselves contributed to find 81 new gene products distributed throughout different categories. The described chromatographic approach provides a significant contribution to the bile protein repertoire and opens new perspectives for the discovery of markers for specific biliary tract diseases.