Identification of low-abundance proteins via fractionation of the urine proteome with weak anion exchange chromatography.

ABSTRACT:

Background

Low-abundance proteins are difficultly observed on the two-dimensional gel electrophoresis (2-DE) maps of urine proteome, because they are usually obscured by high-abundance proteins such as albumin and immunoglobulin. In this study, a novel fractionation method was developed for enriching low-abundance proteins by removing high-abundance proteins and progressive elution with salts of various concentrations.

Results

Stepwise weak anion exchange (WAX) chromatography, which applied DEAE-Sephacel resin with non-fixed volume elution, was used to fractionate urine proteome prior to performing 2-DE. Urine proteome was separated into four fractions by progressively eluting the column with 0 M, 50 mM, 100 mM, and 1 M NaCl solutions. Most of the heavy and light immunoglobu

SUBMITTER: Lu CM 

PROVIDER: S-EPMC3079594 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature