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Comprehensive two‐dimensional chromatography and capillary electrophoresis coupled with tandem time‐of‐flight mass spectrometry for high‐speed proteome analysis
Author(s) -
Zhang Jie,
Hu Hualing,
Gao Mingxia,
Yang Pengyuan,
Zhang Xiangmin
Publication year - 2004
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200405956
Subject(s) - chromatography , capillary electrophoresis , chemistry , mass spectrometry , tandem mass spectrometry , capillary electrophoresis–mass spectrometry , time of flight mass spectrometry , capillary action , proteomics , proteome , analytical chemistry (journal) , ionization , electrospray ionization , materials science , biochemistry , ion , organic chemistry , composite material , gene
A comprehensive two‐dimensional capillary liquid chromatography and capillary zone electrophoresis system coupled with tandem matrix assisted laser desorption/ionization‐time of flight‐time of flight‐mass spectrometry (MALDI‐TOF‐TOF‐MS) proteomics analyzer is presented. Protein/peptide samples were separated by capillary high‐performance liquid chromatography (cHPLC). The effluents from cHPLC (the first dimension) were continuously transferred into capillary zone electrophoresis (CZE, the second dimension) through a novel valve‐free hydrodynamic sampling interface. The CZE effluents were mixed with α‐cyano‐4‐hydroxycinnamic acid (CHCA) matrix sheath flow via CE‐MALDI interface, and then directly deposited on the MALDI target at a 3 s time‐interval for further MS analysis. The high efficiency of the overall system was demonstrated by analysis of proteins in D 20 (human hepatocellular carcinoma model in nude mice with high metastatic potential) liver cancer tissue. More than 300 proteins were identified, which proved the system potential for high‐throughput analysis and application in proteomics.