August 1, 2011.
The definitive version is available at http://dx.doi.org/.
One of the biggest challenges for the study of proteomic biomarkers in blood plasma and blood serum is the broad dynamic range of its protein constituents. For example, 70-95% of all the rat plasma proteins are comprised of albumin, Immunoglobulin (IgG), and transferrin. Therefore, a successful system of proteomic sample preparation to remove these high abundant proteins is needed to examine lower abundant proteins of interest. Researchers have developed successful ways to remove these proteins from human blood samples, but many high abundant protein removal kits for mouse and rat models vary in the efficiency of actual targeted protein content that is removed. In addition, there are different systems for high abundant protein removal, such as antibody based approaches and newer resin/bead based constructs. In this study, three different methods for high abundant protein removal were compared on rat blood plasma and mouse blood serum. In addition, two methods for concentrating and buffer exchange were compared after the high abundant protein removal. Both rodent blood samples were analyzed by the six different method combinations and examined by SDS-PAGE and two-dimensional gel electrophoresis (2-D DIGE).
Center for Biophotonics Science and Technology (CBST)
This material is based upon work supported by the S.D. Bechtel, Jr. Foundation and by the National Science Foundation under Grant No. 0952013. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the authors and do not necessarily reflect the views of the S.D. Bechtel, Jr. Foundation or the National Science Foundation.