作者
Michael T Forrester, Matthew W Foster, Jonathan S Stamler
发表日期
2007/5/11
期刊
Journal of Biological Chemistry
卷号
282
期号
19
页码范围
13977-13983
出版商
Elsevier
简介
Protein S-nitrosylation has emerged as a principal mechanism by which nitric oxide exerts biological effects. Among methods for studying protein S-nitrosylation, the biotin switch technique (BST) has rapidly gained popularity because of the ease with which it can detect individual S-nitrosylated (SNO) proteins in biological samples. The identification of SNO sites by the BST relies on the ability of ascorbate to generate a thiol from an S-nitrosothiol, but not from alternatively S-oxidized thiols (e.g. disulfides, sulfenic acids). However, the specificity of this reaction has recently been challenged, prompting several claims that the BST may produce false-positive results and raising concerns about the application of the BST under oxidizing conditions. Here we perform a comparative analysis of the BST using differentially S-oxidized and S-nitrosylated forms of protein tyrosine phosphatase 1B, as well as intact and lysed …
引用总数
学术搜索中的文章
MT Forrester, MW Foster, JS Stamler - Journal of Biological Chemistry, 2007