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A Prefractionation Method Can Separate Proteomic Proteins into Multigroups by One‐step Extraction
Author(s) -
Bai HaiXin,
Liu XiaoHua,
Yang Fan,
Yang XiuRong,
Wang ErKang
Publication year - 2010
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201000140
Subject(s) - chemistry , chromatography , reagent , proteome , ammonium sulfate , extraction (chemistry) , solubility , protein purification , aqueous solution , biochemistry , organic chemistry
A variety of prefractionation methods for proteome analysis had been developed, but some of these had defects such as requirements sophisticated apparatus, expensive reagents, too long experimental time or complicated operation. In this work, a simple, rapid and low‐cost prefractionation method for proteome analysis was developed based on an aqueous two‐phase system (ATPS), which used simple and inexpensive components in place of the polymers, could pre‐separate proteomic proteins into multigroups by one‐step extraction according proteins' difference in solubility. The ATPS consisted of isopropanol, ammonium sulfate and water. The highlight attractiveness of this method included simplicity, rapidity, low cost and the ability of concentrating target proteins. Attractiveness of this method also included biocompability, amenability to linear scale‐up, potential for continuous operation, and being easy or no need for separating the target proteins from phase‐forming reagents before gel electrophoresis analysis. It was the first time that the ATPS composed of isopropanol, ammonium sulfate and water was used in studying the prefractionation method for proteome analysis. Thus, this method had great significance in proteome analysis and methodology.