Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
ISSN: 0974-276X
Yaojun Li
China
Research Article
Stable Isotope Metabolic Labeling-Based Quantitative Thiol Redox Proteomic
Analysis of Hydrogen Peroxide-treated Arabidopsis plant
Author(s): Qin Hu, Guangyu Guo, Zhu Yang, Yaojun Li, Yiji Xia and Ning LiQin Hu, Guangyu Guo, Zhu Yang, Yaojun Li, Yiji Xia and Ning Li
Homeostasis of protein thiol redox plays an important role in numerous cellular processes and stress responses. The thiol moiety of cysteine residue is easily altered to various redox isoforms that play critical roles in regulation of both structure and function of proteins. In the present study, a quantitative thiol redox proteomic method, termed OxNSIL, has been developed, which integrates the chemical labeling by biotin-tagged alkylating reagents with the heavy nitrogen stable isotope-coded salt metabolic labeling and acquires both advantages of biotin-avidin enrichment and MS-based quantitation of cysteine residue-containing peptides. Both the reduced and the reversibly oxidized cysteine thiol moieties are finally identified in a site-specific manner and measured in a single experiment. Hydrogen peroxide, H2O2, was applied on the whole Arabidopsis plant to trigger thiol redox stat.. View More»
DOI:
10.4172/jpb.1000312