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Analysis of protein redox modification by hypoxia

Authors
Kyoung‐Soo ChoiSoo‐Yeon ParkSun‐Hee BaekRama Dey‐RaoYoung‐Mee ParkZHaitao Zhanghang, HTClement IpEun‐Mi ParkYeul Hong KimJong Hoon Park
Issue Date
Feb-2007
Publisher
TAYLOR & FRANCIS INC
Keywords
hypoxia; oxidative stress; redox modification; proteomics
Citation
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY, v.36, no.1, pp 65 - 79
Pages
15
Journal Title
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY
Volume
36
Number
1
Start Page
65
End Page
79
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/15431
DOI
10.1080/10826060500388520
ISSN
1082-6068
1532-2297
Abstract
We examined hypoxia-induced changes in global thiol proteome profile in human prostate cancer cells using a BIAM-based display method. We analyzed the kinetics of protein thiol modification by using a pattern recognition algorithm, self-organizing maps (SOM) clustering, and identified the BIAM-labeled proteins by MALDI-TOF and ESI-tandem mass spectrometry. We found 99 out of 215 of total BIAM-labeled proteins were affected by hypoxia treatment and, yet, with diverse patterns and kinetics of redox modification. Our study proved that proteomics analysis employing the BIAM-labeling method can provide valuable information pertaining to global changes in the redox status of proteins in response to hypoxia.
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