Identification of heat shock proteins from bacteria by electrophoretic separation and nanoflow LC-MS/MS
Szanics, E.; Devreese, B.; Van Beeumen, J. (2004). Identification of heat shock proteins from bacteria by electrophoretic separation and nanoflow LC-MS/MS. Acta Alimentaria 33(4): 397-404. https://dx.doi.org/10.1556/AAlim.33.2004.4.10
Examination of heat shock and PR (“pathogenesis-related”) proteins is of special interest in food science. Many food allergens have a similar or the same structure as PR proteins, which are produced in the plants as a response to pathogenesis or certain environmental stresses. The protein set of the psychrophilic bacterium Shewanella hanedai was studied by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). Gel patterns from control and heat-treated bacteria were evaluated by PDQUEST software. The differentially expressed proteins were excised from the gel and digested by trypsin. The tryptic peptides were analysed by nanoflow LC-MS/MS. On the basis of amino acid sequences obtained by this method, the proteins were identified by similarity searching in the protein database. Using this proteomic approach a heat shock and a 50S ribosomal protein were identified as the major heat induced proteins in Shewanella hanedai.
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