Abstract
The presence of affinity reagents such as immunoglobulin in preparations for sensitive mass spectrometry analyses can preclude the identification of low-abundance proteins of interest. We report a method whereby antisera are purified and biotinylated prior to use in immunoprecipitation that allows for its efficient removal from proteomic samples via streptavidin capture. This method can similarly be extended to other affinity reagents such as recombinant fusion proteins for enhanced identification of interacting proteins.
Original language | English |
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Pages (from-to) | 4758-4762 |
Number of pages | 5 |
Journal | Journal of Proteome Research |
Volume | 6 |
Issue number | 12 |
DOIs | |
State | Published - Dec 2007 |
Keywords
- Biotin
- Immunoprecipitation
- Mass spectrometry
- Streptavidin
- Toxoplasma
ASJC Scopus subject areas
- General Chemistry
- Biochemistry