Affinity purification-mass spectrometry - Powerful tools for the characterization of protein complexes

被引:173
作者
Bauer, A [1 ]
Kuster, B [1 ]
机构
[1] Cellzome AG, D-69117 Heidelberg, Germany
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 2003年 / 270卷 / 04期
关键词
TAP (tandem affinity purification);
D O I
10.1046/j.1432-1033.2003.03428.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Multi-protein complexes are emerging as important entities of biological activity inside cells that serve to create functional diversity by contextual combination of gene products and, at the same time, organize the large number of different proteins into functional units. Many a time, when studying protein complexes rather than individual proteins, the biological insight gained has been fundamental, particularly in cases in which proteins with no previous functional annotation could be placed into a functional context derived from their 'molecular environment'. In this minireview, we summarize the current state of the art for the retrieval of multiprotein complexes by affinity purification and their analysis by mass spectrometry. The advances in technology made over the past few years now enable the study of protein complexes on a proteomic scale and it can be anticipated that the knowledge gathered from such projects will fuel drug target discovery and validation pipelines and that the technology is also going to prove valuable in the emerging field of systems biology.
引用
收藏
页码:570 / 578
页数:9
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