Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry (2002)
| Venue: | Mol. Cell. Proteomics |
| Citations: | 12 - 1 self |
BibTeX
@ARTICLE{Adkins02towarda,
author = {Joshua N. Adkins and Susan M. Varnum and Kenneth J. Auberry and Ronald J. Moore and Nicolas H. Angell and Richard D. Smith and David L. Springer and Joel G. Pounds},
title = {Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry},
journal = {Mol. Cell. Proteomics},
year = {2002},
volume = {1},
pages = {947--955}
}
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Abstract
Blood serum is a complex body fluid that contains various proteins ranging in concentration over at least 9 orders of magnitude. Using a combination of mass spectrometry technologies with improvements in sample preparation, we have performed a proteomic analysis with submilliliter quantities of serum and increased the measurable concentration range for proteins in blood serum beyond previous reports. We have detected 490 proteins in serum by on-line 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 strong cation exchange chromatography into distinct fractions prior to analysis. This separation resulted in a
