期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1216, 期 8, 页码 1241-1252出版社
ELSEVIER
DOI: 10.1016/j.chroma.2008.11.051
关键词
Egg yolk; Peptide libraries; Hexapeptide ligands; Low-abundance proteome; Mass spectrometry
资金
- Fondazione Cariplo (Milan, Italy)
- PRIN 2006 (MURST, Rome, Italy)
- Bilateral Project Novel Methods for Top-down Analysis of Macromolecular and Nanosized Samples of Biotechnological and Environmental Interest
- VIII Executive Programme of Scientific and Technological Cooperation between Italy and Korea for the years 2007-2009
- Fondazione Cariplo
The use of combinatorial peptide ligand libraries (CPLLs), containing hexapeptides terminating with a primary amine, or modified with a terminal carboxyl group, or with a terminal tertiary amine. allowed discovering and identifying a large number of previously unreported egg yolk proteins. Whereas the most comprehensive list up to date [K. Mann, M. Mann, Proteomics, 8 (2008) 178-191] tabulated about 115 unique gene products in the yolk plasma, our findings have more than doubled this value to 255 unique protein species. From the initial non-treated egg yolk it was possible to find 49 protein species; the difference was generated thanks to the use of the three combined CPLLs. The aberrant behaviour of some proteins, upon treatment via the CPLL method, such as proteins that do not interact with the library, is discussed and evaluated. Simplified elution protocols from the CPLL beads are taken into consideration, of which direct elution in a single step via sodium dodecyl sulphate desorption seems to be quite promising. Alternative methods are suggested. The list of egg yolk components here reported is by far the most comprehensive at present and could serve as a starting point for isolation and functional characterization of proteins possibly having novel pharmaceutical and biomedical applications. (c) 2008 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据