期刊
PROTEOMICS
卷 5, 期 4, 页码 840-842出版社
WILEY
DOI: 10.1002/pmic.200401056
关键词
in-gel digestion; microwave
Proteomics characterizes cellular proteins and their abundance, state of modification, protein complexes and interactions [1]. The global changes in cellular protein expression can be visualized by 1-D or 2-DE and identified by MS [2]. Peptide identification can be accomplished by peptide mass mapping. The first step is the in-gel digestion of proteins by sequence-specific proteases. Since each amino acid residue has a unique mass, protein digestion will yield a set of distinct peptides specific to each protein. A mass spectrum of digested peptides, therefore, results in a unique PMF. The set of peptide masses obtained by MS is then used to search against protein databases created by in silico cleavage of all known sequences [3]. This method has been shown to be particularly successful for the identification of proteins [1, 4-6]. However, it is limited by its inability to speed up the in-gel digestion process.
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