Enrichment and Identification of Cysteine-Containing Peptides from Tryptic Digests of Performic Oxidized Proteins by Strong Cation Exchange LC and MALDI-TOF/TOF MS
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- 作者：Jingquan Dai ; Jinglan Wang ; Yangjun Zhang ; Zhuang Lu ; Bing Yang ; Xiaohai Li ; Yun Cai ; and Xiaohong Qian
- 刊名：Analytical Chemistry
- 出版年：2005
- 出版时间：December 1, 2005
- 年：2005
- 卷：77
- 期：23
- 页码：7594 - 7604
- 全文大小：1582K
- 年卷期：v.77,no.23(December 1, 2005)
- ISSN：1520-6882
文摘
The extreme complexity of sample and uninformativefragmentation of peptides in MS/MS experiments are twoof several real challenges faced by proteomics. In thiswork, a strategy aimed at tackling these two problems ispresented. Briefly, proteins were first oxidized by performic acid to cleave the disulfide bonds and simultaneouslyconvert cysteine residue into its sulfonic form. Then theresultant sulfonic peptides were enriched by SCX chromatography, exploiting the negative solution charge ofsulfonic group. The sulfonic peptide could be easilydetected by MALDI-MS in negative mode and showedboth enhanced fragmentation efficiency and a simplifiedspectrum in MALDI-MS/MS experiment in positive mode.The strength of the strategy was demonstrated by applyingit to bovine serum albumin. Potential use of the strategyin proteomics was also discussed.