Abstract:

Objective     To establish and evaluate a method of depleting high-abundant proteins for cerebrospinal fluid (CSF) in two-dimensional electrophoresis(2-DE) analysis. Methods     The CSF sample pool was concentrated to an appropriate volume by ultrafiltration, and then high-abundant proteins were depleted with the commercial Albumin and IgG Removal Kit designed for serum. The remaining CSF containing low-abundant proteins was precipitated by acetone and used for 2-DE analysis and 2-DE Western blot identification. Results      Most high-abundant proteins could be depleted with this method. The following 2-DE analysis revealed that low-abundant proteins were obviously enriched after the depletion of high-abundant proteins. Compared with the results of 2-DE Western blot, depleting high-abundant proteins enabled the 3 different fragments of tetranectin visible in 2-DE map. Conclusion    The high-abundant protein depletion method for CSF established in this study is simply performable, and can be helpful in the detection of low-abundant proteins in 2-DE analysis.

Key words: Cerebrospinal fluid; Electrophoresis，gel，two-dimensional; High-abundant protein; Two-dimensional electrophoresis western blot