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Updated: Aug 8, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Redox proteomics in the mussel, Mytilus edulis
B McDonagh1, R Tyther, D Sheehan
1Proteomics Research Group, Department of Biochemistry, Environmental Research Institute, University College Cork, Lee Maltings, Prospect Row, Mardyke, Cork, Ireland.
Abstract:
Pollutants (e.g. PAHs, metals) cause oxidative stress (OS) by forming reactive oxygen species. Redox proteomics provides a means for identifying protein-specific OS effects in Mytilus edulis. Groups of mussels were sampled from a clean site in Cork Harbour, Ireland and exposed to 1 mM H2O2 in holding tanks. Protein extracts of gill and digestive gland were separated by two dimensional electrophoresis and similar protein expression profiles were found. Effects of OS on disulphide bridge patterns were investigated in diagonal gels by separating proteins in non-reducing conditions followed by a second reducing dimension. Immunoprecipitation selected carbonylated and glutathionylated proteins. These methodologies can contribute to redox proteomic studies of pollutant responses in marine organisms.
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