Protein Cysteinyl-S-Nitrosylation: Analysis and Quantification

J. E. Wiktorowicz, S. J. Stafford, N. J. Garg

Research output: Chapter in Book/Report/Conference proceedingChapter

9 Scopus citations


The thiol moiety of cysteine residues can undergo a number of biologic modifications including oxidation, sulfenylation, nitrosylation, persulfidation, metalation, and other modifications. These modifications can control biological function, including gain as well as loss of function. Herein, we focus attention on the proteomic analysis of S-nitrosylation in health and disease. We describe a novel quantitative approach that combines accurate, sensitive fluorescence modification of cysteinyl-S-nitrosylation that leaves electrophoretic mobility unaffected (SNOFlo), and introduce unique concepts for measuring changes in S-nitrosylation status relative to protein abundance. We present several studies where suitability of this approach for investigating endogenous S-nitrosylation is addressed.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Number of pages14
StatePublished - 2017

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • BODIPY Fl-maleimide
  • Cysteinyl-S-nitrosylation
  • Proteome

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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