Deep insights into the plant proteome by pretreatment with combinatorial hexapeptide ligand libraries

被引:15
作者
Froehlich, Andreas [1 ]
Lindermayr, Christian [1 ]
机构
[1] German Res Ctr Environm Hlth, Helmholtz Zentrum Munchen, Inst Biochem Plant Pathol, D-85764 Neuherberg, Germany
关键词
Low abundant proteins; ProteoMiner; Sample fractionation; Combinatorial hexapeptide libraries; Dynamic range; Plant proteome; LOW-ABUNDANCE PROTEOME; IN-DEPTH EXPLORATION; RED-BLOOD-CELLS; PEPTIDE LIBRARIES; CYTOPLASMIC PROTEOME; LATEX ALLERGENS; TECHNOLOGY; PROTEINS; IDENTIFICATION; BEADS;
D O I
10.1016/j.jprot.2011.02.019
中图分类号
Q5 [生物化学];
学科分类号
070307 [化学生物学];
摘要
Proteome analyses suffer from the large complexity of even small proteomes. Additionally, in many protein samples a few highly abundant proteins are hindering detailed proteomic studies, since they mask low abundant proteins. Recently, a new technology has emerged, which reduces dynamic range of protein concentrations within a given sample using combinatorial hexapeptide ligand libraries (CPLLs). This technique has been widely used in the microbial, animal and human fields and is now going to enter plant research. It can be a useful tool for fractionation of protein samples and might help to get a deeper insight into specific plant proteomes. In this review we describe the CPLL protein fractionation, summarize its possible applications in the plant field and discuss the limitations of this method. (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码:1182 / 1189
页数:8
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