由精氨酸残基界定的无赖氨酸胰蛋白酶肽段的选择性分离：蛋白质组分析的一种新工具。

Selective isolation of lysine-free tryptic peptides delimited by arginine residues: A new tool for proteome analysis.

作者信息

Sánchez Aniel, González Luis J, Ramos Yassel, Betancourt Lazaro, Gil Jeovanis, Besada Vladimir, Fernández-de-Cossio Jorge, Alvarez Félix, Padrón Gabriel

机构信息

Mass Spectrometry Laboratory, Department of Proteomics, Center for Genetic Engineering and Biotechnology, P.O. Box 6162, Havana, Cuba.

出版信息

J Proteome Res. 2006 May;5(5):1204-13. doi: 10.1021/pr060003w.

DOI:10.1021/pr060003w

PMID:16674110

Abstract

Tryptic digestion of biotinylated Lys-C peptides followed by affinity chromatography allows the selective isolation of lysine-free tryptic peptides delimited by arginine residues (RRnK peptides). In silico analysis revealed that RRnK peptides represent 87% of the whole proteomes and their specific isolation simplifies the complex peptide mixture (5 peptides per protein). The good recoveries and high selectivity obtained in the isolation of RRnK peptides anticipate the applicability of this method in 2DE-free quantitative proteome analyses.

摘要

对生物素化的赖氨酸-C肽进行胰蛋白酶消化，然后进行亲和色谱分离，可选择性分离由精氨酸残基界定的无赖氨酸胰蛋白酶肽（RRnK肽）。计算机分析表明，RRnK肽占整个蛋白质组的87%，其特异性分离简化了复杂的肽混合物（每个蛋白质5个肽）。在RRnK肽分离中获得的良好回收率和高选择性预示着该方法在无二维电泳定量蛋白质组分析中的适用性。