A RAPID APPROACH FOR THE DETECTION, QUANTIFICATION, AND DISCOVERY OF NOVEL SULFENIC ACID OR S-NITROSOTHIOL MODIFIED PROTEINS USING A BIOTIN-SWITCH METHOD

被引：39

作者：

Burgoyne, Joseph R. ^{[1
]}

Eaton, Philip ^{[1
]}

机构：

[1] Kings Coll London, Div Cardiovasc, Dept Cardiol, St Thomas Hosp,Rayne Inst, London WC2R 2LS, England

来源：

METHODS IN ENZYMOLOGY, VOL 473: THIOL REDOX TRANSITIONS IN CELL SIGNALING, PT A: CHEMISTRY AND BIOCHEMISTRY OF LOW MOLECULAR WEIGHT AND PROTEIN THIOLS | 2010年 / 473卷

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

NITRIC-OXIDE SYNTHASE; TYROSINE-PHOSPHATASE; 1B; HYDROGEN-PEROXIDE; REDOX REGULATION; NADPH OXIDASES; MOLECULAR REGULATION; RYANODINE RECEPTOR; CELL-PROLIFERATION; ENDOTHELIAL-CELLS; OXIDATIVE STRESS;

D O I：

10.1016/S0076-6879(10)73015-9

中图分类号：

Q5 [生物化学];

学科分类号：

070307 [化学生物学];

摘要：

The recent development of robust methods for the detection of proteins susceptible to S-nitrosylation (RSNO) and sulfenation (RSOH) has provided greater insight into the role of these oxidative modifications in cell signaling. These techniques, which have been termed "biotin-switch" methods, essentially use selective chemical reduction to swap an oxidative modification for a stable easily detectable biotin-tag. This allows for the rapid purification and subsequent detection of modified proteins using mass spectrometry. This chapter provides an overview of these biotin-switch methods, and explores its impact on the field of redox biology, including recent advances as well as limitations associated with this technique.

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收藏

页码：281 / 303

页数：23

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