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Submitted on October 2, 2002
Revised on November 13, 2002
Accepted on November 15, 2002

Toward a human blood serum proteome: Analysis by multidimensional separation coupled with mass spectrometry

Joshua N. Adkins, Susan M. Varnum, Kenneth J. Auberry, Ronald J. Moore, Nicolas H. Angell, Richard D. Smith, David L. Springer, and Joel G. Pounds

Molecular Biosciences Dept, Pacific Northwest National Laboratory, Richland, WA 99352

Corresponding Author: joel.pounds{at}pnl.gov

Blood serum is a complex bodily fluid that contains proteins ranging in concentrations over at least nine orders of magnitude. Using a combination of powerful mass spectrometry technologies with improvements in sample preparation, we have performed a proteomic analysis with sub-mL quantities of serum, and increased the measurable concnetration range for proteins in blood serum beyond previous reports. We have detected 490 proteins in serum by online reversed-phase microcapillary liquid chromatography coupled with ion trap mass spectrometry. To perform this analysis, immunoglobulins were removed from serum using protein A/G, and the remaining proteins were digested with trypsin. Resulting peptides were separated by stron-cation exchange chromatography into distinct fraction prior to analysis. This separation resulted in an increase in the number of proteins detected in an individual serum sample by 3 to 5 fold. With this increase in the number of proteins identified, we have detected some lower abundance serum proteins (ng/mL range) including human growth hormone, interleukin-12, and prostate-specific antigen. With this study, we have performed the most extensive analysis of serum proteins to date and laid the foundation for future refinements in the identification of novel protein biomarkers of disease.


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