Romancing the “hidden proteome”, Anno Domini two zero zero seven

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• 作者：Egisto Boschetti ; Lee Lomas ; Attilio Citterio ; Pier Giorgio Righetti
• 关键词：Ligand library ; Peptide ligands ; SELDI-mass spectrometry ; Low-abundance proteome
• 刊名：Journal of Chromatography A
• 出版年：2007
• 期刊代码：47_00219673
• 类别：ch
• 出版时间：15 June 2007
• 卷：1153
• 期：1-2
• 页码：277-290
• 文件大小：1553 K

摘要

The mechanism of action and properties of a solid-phase ligand library made of hexapeptides, for capturing the “hidden proteome”, i.e. the low- and very low-abundance proteins constituting the vast majority of species in any proteome, be it a cell or tissue lysate or a biological fluid, are here reviewed. Mechanisms of adsorption are evaluated, as well as different protocols for en bloc or sequential elution of the captured polypeptides. Examples are given of capture of proteins from serum, human platelet extracts, bacterial extract and egg white. The increment in detection of low-abundance species appears to be of at least four-fold as compared with untreated samples. One particular aspect of this capture is the adsorption of a high proportion of small peptides (in the Mr 600–8000 Da range) that are normally lost upon electrophoretic two-dimensional mapping. Such a peptide population, in human sera, may be of particular importance since it may contain protein cleavage products of diagnostic value.