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Published on: August 7, 2014
Heparin chromatography to deplete high-abundance proteins for serum proteomics
Ting Lei1, Qing-Yu He, Yi-Li Wang
1Institute of Cancer Research, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an, China.
Background:
Serum is a very informative sample for disease diagnosis. However, a few of the high-abundance proteins existing in serum make the identification of disease-specific serum biomarkers extremely challenging using currently available technologies. A highly promising first step for most analytical approaches of serum is to deplete as many of the high-abundance proteins as possible.
Methods:
We introduced the traditional method of heparin chromatography coupled with protein G sepharose to deplete the high-abundance proteins for serum proteomics.
Results:
Compared with the multiple affinity removal system (MARS) column (a commercial version to deplete 6 major proteins in serum), heparin chromatography can deplete more high-abundance proteins in a single step, especially many high molecular-weight proteins. Using this simple and inexpensive method to pretreat serum for 2-DE analysis, more protein spots can be visualized. IgGs depletion by protein G sepharose can further enhance the resolution of the resulting serum proteome.
Conclusions:
Heparin chromatography coupled with protein G appears to be an efficient and economical strategy to pretreat serum for serum proteomics.
