| Literature DB >> 17379583 |
Andrew Gow1, Allan Doctor, Joan Mannick, Benjamin Gaston.
Abstract
S-Nitrosothiol (SNO) cysteine modifications are regulated signaling reactions that dramatically affect, and are affected by, protein conformation. The lability of the SNO 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.Entities:
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Year: 2007 PMID： 17379583 PMCID： PMC1949323 DOI： 10.1016/j.jchromb.2007.01.052
Source DB: PubMed Journal: J Chromatogr B Analyt Technol Biomed Life Sci ISSN： 1570-0232 Impact factor: 3.205