Covalent selection of the thiol proteome on activated thiol sepharose: A robust tool for redox proteomics

• Published in: Talanta (Oxford) Vol. 80; no. 4; pp. 1569 - 1575
• Main Authors: Hu, Wentao, Tedesco, Sara, Faedda, Roberto, Petrone, Goffredo, Cacciola, Santa Olga, O’Keefe, Anne, Sheehan, David
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 15.02.2010
• Subjects: Activated thiol sepharose; Animals; Antioxidants; Bivalvia; Cysteine; Cysteine - metabolism; Disulfides - metabolism; Escherichia coli; Glutathione - metabolism; Mytilus edulis; Oxidation-Reduction; Oxidative Stress; Proteome - chemistry; Proteomics - methods; Reactive Oxygen Species; Redox proteomics; Sepharose - analogs & derivatives; Sepharose - chemistry; Sulfhydryl Compounds - chemistry; Sulfhydryl Compounds - metabolism; Thiol-containing proteins; Trichoderma harzianum; Trichoderma harzianum; Oxidative stress; Redox proteomics; Cysteine; Mytilus edulis; Escherichia coli; Thiol-containing proteins; Activated thiol sepharose

Protein thiols contribute significantly to antioxidant defence and selective oxidation of cysteines is important in signal transduction even in sub-stress scenarios. However, cysteine is the second rarest residue in proteins and it can be difficult to target low-abundance thiol (–SH)-containing prot...