Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture

被引：310

作者：

Forrester, Michael T. ^{[1
,2
]}

Thompson, J. Will ^{[3
]}

Foster, Matthew W. ^{[4
]}

Nogueira, Leonardo ^{[4
]}

Moseley, M. Arthur ^{[3
]}

Stamler, Jonathan S. ^{[1
,4
]}

机构：

[1] Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA

[2] Duke Univ, Med Ctr, Med Scientist Training Program, Durham, NC 27710 USA

[3] Duke Univ, Med Ctr, Prote Core Facil, Durham, NC 27710 USA

[4] Duke Univ, Med Ctr, Dept Med, Durham, NC 27710 USA

来源：

NATURE BIOTECHNOLOGY | 2009年 / 27卷 / 06期

基金：

美国国家卫生研究院;

关键词：

IDENTIFICATION;

D O I：

10.1038/nbt.1545

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

We have modified the biotin switch assay for protein S-nitrosothiols (SNOs), using resin-assisted capture (SNO-RAC). Compared with existing methodologies, SNO-RAC requires fewer steps, detects high-mass S-nitrosylated proteins more efficiently, and facilitates identification and quantification of S-nitrosylated sites by mass spectrometry. When combined with iTRAQ labeling, SNO-RAC revealed that intracellular proteins may undergo rapid denitrosylation on a global scale. This methodology is readily adapted to analyzing diverse cysteine-based protein modifications, including S-acylation.

引用

页码：557 / 559

页数：3

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