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

MUIR > Graduate Institute of Health Care > Department of Beauty Science > Papers > Item 987654321/1230

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Title:	Identification of low-abundance proteins via fractionation of the urine proteome with weak anion exchange chromatography
Authors:	Chih-Ming Lu;Yu-Jen Wu;Cheng-Chi Chen;Jue-Liang Hsu;Jiing-Chuan Chen;Jeff Yi-Fu Chen;Chun-Hsiung Huang;Ying-Chin Ko
Keywords:	Weak anion exchange chromatography DEAE-Sephacel;Fractionation;Proteomic;Urine
Date:	2011-04
Issue Date:	2011-09-28T03:58:03Z (UTC)
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 nonfixed 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 immunoglobulin chains appeared in the eluent. After the high-abundance proteins were removed, various low-abundance proteins were enriched and could be easily identified. The potential of this method for obtaining diversified fractionations was demonstrated by eluting the column separately with Na2SO4 and MgCl2 solutions. The 2-DE maps of the fractions eluted with these different salt solutions of identical ionic strength revealed markedly different stain patterns. Conclusion: The present study demonstrated that this fractionation method could be applied for purposes of enriching low-abundance proteins and obtaining diversified fractionations of urine, and potentially other proteomes.
Relation:	Proteome Sci. 2011 Apr 8;9:17
Appears in Collections:	[Department of Beauty Science] Papers

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