Protein Cysteinyl-S-Nitrosylation: Analysis and Quantification

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

    Research output: Chapter in Book/Report/Conference proceedingChapter

    4 Scopus citations

    Abstract

    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.
    Pages1-14
    Number of pages14
    Volume586
    DOIs
    StatePublished - 2017

    Publication series

    NameMethods in Enzymology
    Volume586
    ISSN (Print)00766879
    ISSN (Electronic)15577988

    Keywords

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

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology

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  • Cite this

    Wiktorowicz, J. E., Stafford, S. J., & Garg, N. (2017). Protein Cysteinyl-S-Nitrosylation: Analysis and Quantification. In Methods in Enzymology (Vol. 586, pp. 1-14). (Methods in Enzymology; Vol. 586). Academic Press Inc.. https://doi.org/10.1016/bs.mie.2016.10.016