详细信息
Zirconium-Cation-Immobilized Core/Shell (Fe3O4@Polymer) Microspheres as an IMAC Material for the Selective Enrichment of Phosphopeptides ( SCI-EXPANDED收录) 被引量:17
文献类型:期刊文献
英文题名:Zirconium-Cation-Immobilized Core/Shell (Fe3O4@Polymer) Microspheres as an IMAC Material for the Selective Enrichment of Phosphopeptides
作者:Zheng, Leyou[2];Dong, Huaping[1];Hu, Liujiang[1]
机构:[1]Shaoxing Univ, Coll Chem & Chem Engn, Shaoxing 312000, Zhejiang, Peoples R China;[2]NHU Co Ltd Zhejiang, Xinchang 312500, Zhejiang, Peoples R China
年份:2013
卷号:52
期号:23
起止页码:7729
外文期刊名:INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH
收录:SCI-EXPANDED(收录号:WOS:000320484300015)、、WOS
基金:This work was supported by the Natural Science Foundation of Zhejiang Province, China (LY12B06003), and the Science and Technology Program of Shaoxing (2011A21056).
语种:英文
外文关键词:Affinity chromatography - Biocompatibility - Biosynthesis - Casein - Iron oxides - Magnetite - Mass spectrometry - Microspheres - Proteins - Sodium chloride - Urea
外文摘要:Immobilized metal affinity chromatography (IMAC) is a widely employed method for the enrichment of phosphopeptides from complex proteolytic digests prior to mass spectrometric analysis. In this work, a novel IMAC material, zirconium-phosphate (Zr4+-PO3)-modified magnetic Fe3O4/GMA-co-EDMA (core/shell) (Zr4+-Fe3O4@polymer) microspheres, has been synthesized in a facile manner and used for the selective capture of phosphopeptides from protein tryptic digests for mass spectrometry analysis. The enrichment conditions were optimized using a protein digest solution of beta-casein. By virtue of a thick and biocompatible poly(GMA-co-EDMA) shell, high tolerance of contaminants (salt, nonphosphopeptide) was demonstrated for the use of Zr4+-Fe3O4@polymer microspheres for the highly selective enrichment of phosphopeptides from a protein tryptic solution that contained a high concentration of NaCl (6.2 M) or urea (8,M) and a high ratio of nonphosphoprotein (BSA) to phosphoprotein (alpha-casein) (1:500). The performance of the Zr4+-Fe3O4@polymer microspheres was further successfully examined by the phosphoproteome analysis of mouse liver lysate.
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