S-Nitrosothiol measurements in biological systems

Andrew Gow, Allan Doctor, Joan Mannick, Benjamin Gaston

Research output: Contribution to journalReview article

90 Scopus citations

Abstract

S-Nitrosothiol (SNO) cysteine modifications are regulated signaling reactions that dramatically affect, and are affected by, protein conformation. The lability of the S{single bond}NO bond can make SNO-modified proteins cumbersome to measure accurately. Here, we review methodologies for detecting SNO modifications in biology. There are three caveats. (1) Many assays for biological SNOs are used near the limit of detection: standard curves must be in the biologically relevant concentration range. (2) The assays that are most reliable are those that modify SNO protein or peptide chemistry the least. (3) Each result should be quantitatively validated using more than one assay. Improved assays are needed and are in development.

Original languageEnglish
Pages (from-to)140-151
Number of pages12
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume851
Issue number1-2
DOIs
StatePublished - May 15 2007

Keywords

  • Cysteine
  • Reviews
  • S-Nitrosoglutathione
  • S-Nitrosohemoglobin
  • S-Nitrosylation
  • Signaling

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