ArticleMolecular & cellular proteomics : MCP2009
Artifactual sulfation of silver-stained proteins: implications for the assignment of phosphorylation and sulfation sites.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Are Sulfates of the Hydroxyl Amino Acids Threonine and Serine Truly Extremely Rare or Do They Simply Escape Detection?Life (Basel, Switzerland) · 2026Article
- Review
- Common errors in mass spectrometry-based analysis of post-translational modifications.Proteomics · 2016Review
- Surfactant-Induced Artifacts during Proteomic Sample Preparation.Analytical chemistry · 2015Article
- Tyrosine sulfation as a protein post-translational modification.Molecules (Basel, Switzerland) · 2015Review
- Systematic analysis of the in situ crosstalk of tyrosine modifications reveals no additional natural selection on multiply modified residues.Scientific reports · 2014Article
- Regulation of the histone deacetylase Hst3 by cyclin-dependent kinases and the ubiquitin ligase SCFCdc4.The Journal of biological chemistry · 2014Article
- Simultaneous identification of tyrosine phosphorylation and sulfation sites utilizing tyrosine-specific bromination.Journal of the American Society for Mass Spectrometry · 2011Article
- Article
- Novel oxidative modifications in redox-active cysteine residues.Molecular & cellular proteomics : MCP · 2011Article
- Proteomics analysis of the cardiac myofilament subproteome reveals dynamic alterations in phosphatase subunit distribution.Molecular & cellular proteomics : MCP · 2010Article
- Mechanistic insights into nitrite-induced cardioprotection using an integrated metabolomic/proteomic approach.Circulation research · 2009Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sulfation and phosphorylation are post-translational modifications imparting an isobaric 80-Da addition on the side chain of serine, threonine, or tyrosine residues. These two post-translational modifications are often difficult to distinguish because of their similar MS fragmentation patterns. Targeted MS identification of these modifications in specific proteins commonly relies on their prior separation using gel electrophoresis and silver staining. In the present investigation, we report a potential pitfall in the interpretation of these modifications from silver-stained gels due to artifactual sulfation of serine, threonine, and tyrosine residues by sodium thiosulfate, a commonly used reagent that catalyzes the formation of metallic silver deposits onto proteins. Detailed MS analyses of gel-separated protein standards and Escherichia coli cell extracts indicated that several serine, threonine, and tyrosine residues were sulfated using silver staining protocols but not following Coomassie Blue staining. Sodium thiosulfate was identified as the reagent leading to this unexpected side reaction, and the degree of sulfation was correlated with increasing concentrations of thiosulfate up to 0.02%, which is typically used for silver staining. The significance of this artifact is discussed in the broader context of sulfation and phosphorylation site identification from in vivo and in vitro experiments.
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