S-nitrosothiol measurements in biological systems

被引:103
作者
Gow, Andrew
Doctor, Allan
Mannick, Joan
Gaston, Benjamin
机构
[1] Rutgers State Univ, Sch Pharmacol & Toxicol, Piscataway, NJ 08854 USA
[2] Washington Univ, Dept Pediat, St Louis, MO 63110 USA
[3] Washington Univ, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA
[4] Univ Massachusetts, Sch Med, Dept Internal Med, Worcester, MA 01655 USA
[5] Univ Virginia, Dept Pediat, Charlottesville, VA 22908 USA
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2007年 / 851卷 / 1-2期
关键词
reviews; S-nitrosoglutathione; S-nitrosylation; S-Nitrosohemoglobin; signaling; cysteine;
D O I
10.1016/j.jchromb.2007.01.052
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
S-Nitrosothiol (SNO) cysteine modifications are regulated signaling reactions that dramatically affect, and are affected by, protein conformation. The lability of the S-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. (C) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:140 / 151
页数:12
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