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A colorimetric assay for sulfiredoxin activity using inorganic phosphate measurement

Title
A colorimetric assay for sulfiredoxin activity using inorganic phosphate measurement
Authors
Kim H.Hong S.Rhee S.G.Jeong W.
Ewha Authors
이서구정우진
SCOPUS Author ID
이서구scopusscopus; 정우진scopus
Issue Date
2009
Journal Title
Analytical Biochemistry
ISSN
0003-2697JCR Link
Citation
Analytical Biochemistry vol. 393, no. 1, pp. 36 - 40
Indexed
SCIE; SCOPUS WOS scopus
Document Type
Article
Abstract
2-Cys peroxiredoxin (Prx) is the major subgroup of a family of Prx enzymes that reduce peroxide molecules such as hydrogen peroxide (H2O2). 2-Cys Prxs are inactivated when their active site cysteine residue is hyperoxidized to sulfinic acid. Sulfiredoxin (Srx) is an enzyme that catalyzes reduction of hyperoxidized 2-Cys Prxs in the presence of ATP, Mg2+, and thiol equivalent. Therefore, Srx activity is crucial for cellular function of 2-Cys Prxs. The method currently available for the determination of Srx activity relies on immunoblot detection using antibodies to hyperoxidized enzymes. Here we introduce a simple quantitative assay for Srx activity based on the colorimetric determination of inorganic phosphate released in Srx-dependent reduction of hyperoxidized Prx using the malachite green. The colorimetric assay was used for high-throughput screening of 25,000 chemicals to find Srx inhibitors. © 2009 Elsevier Inc. All rights reserved.
DOI
10.1016/j.ab.2009.06.030
Appears in Collections:
일반대학원 > 생명·약학부 > Journal papers
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