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KMID : 0380219990320020168
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Journal of Biochemistry and Molecular Biology
1999 Volume.32 No. 2 p.168 ~ p.172
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Thioredoxin in the Periplasmic Space of Escherichia coli as a Physiological Electron Donor to Periplasmic Thiol Peroxidase, p20
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Cha Mee-Kyung
Kim Il-Han
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Abstract
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We previously reported that a novel thiol peroxidase (p20) from Escherichia coli is a distinct periplasmic peroxidase that detoxifies hydroperoxides together with glutathione or thioredoxin. Until now, there was no experimental evidence for the presence of thioredoxin (Trx) in the periplasmic space. In an attempt to confirm the physiological function of p20 as a thiol peroxidase supported by Trx in the periplasmic space, we have purified a Trx activity from the periplasmic space of Escherichia coli and identified the Trx as the same protein as the cytoplasmic Trx. The presence of Trx in the periplasmic space of Escherichia coli suggests that p20 is a unique extracellular Trx-linked thiol peroxidase.
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KEYWORD
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Eschericia coli, Periplasmic Space, Thiol Peroxidase, Thioredoxin, Translocation
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