Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이서구 | * |
dc.contributor.author | 강상원 | * |
dc.date.accessioned | 2018-05-18T08:15:13Z | - |
dc.date.available | 2018-05-18T08:15:13Z | - |
dc.date.issued | 2005 | * |
dc.identifier.issn | 0003-2697 | * |
dc.identifier.other | OAK-2636 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/243183 | - |
dc.description.abstract | 2-Cys peroxiredoxin (Prx) is a novel cellular peroxidase that reduces peroxides in the presence of thioredoxin, thioredoxin reductase, and nicotinamide adenine dinucleotide phosphate (NADPH) and that functions in H 2O2-mediated signal transduction. Recent studies have shown that 2-cys Prx can be inactivated by cysteine overoxidation in conditions of oxidative stress. Therefore, peroxidase activity, rather than the protein level, of 2-cys Prx is the more important measure to predict its cellular function. Here, we introduce a modified activity assay method for mammalian 2-cys Prx based on yeast nonselenium thioredoxin reductase. Yeast thioredoxin reductase is expressed in Escherichia coli cells and purified at high yield (40 mg/L of culture broth) as an active flavoprotein by combined diethyl aminoethyl (DEAE) and phenyl hydrophobic chromatography. The optimal concentrations of yeast thioredoxin and thioredoxin reductase required to achieve maximum mammalian 2-cys Prx activity are 3.0 and 1.5 μM, respectively. This modified assay method is useful for measuring 2-cys Prx activity in cell lysates and can also be adapted for a 96-well plate reader for high-throughput screening of chemical compounds that target 2-cys Prx. © 2004 Elsevier Inc. All rights reserved. | * |
dc.language | English | * |
dc.title | Activity assay of mammalian 2-cys peroxiredoxins using yeast thioredoxin reductase system | * |
dc.type | Article | * |
dc.relation.issue | 2 | * |
dc.relation.volume | 338 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 216 | * |
dc.relation.lastpage | 236 | * |
dc.relation.journaltitle | Analytical Biochemistry | * |
dc.identifier.doi | 10.1016/j.ab.2004.12.008 | * |
dc.identifier.wosid | WOS:000227750900006 | * |
dc.identifier.scopusid | 2-s2.0-14644394199 | * |
dc.author.google | Kim J.-A. | * |
dc.author.google | Park S. | * |
dc.author.google | Kim K. | * |
dc.author.google | Rhee S.G. | * |
dc.author.google | Kang S.W. | * |
dc.contributor.scopusid | 이서구(7401852092) | * |
dc.contributor.scopusid | 강상원(55731433900) | * |
dc.date.modifydate | 20240423081003 | * |