Characterization of Helicobacter pylori adhesin thiol peroxidase (HP0390) purified from Escherichia coli

Authors
Nguyen, Huyen Thi MinhNam, Kwang-HoSaleem, YasarKim, Key-Sun
Issue Date
2010-06
Publisher
INDIAN ACAD SCIENCES
Citation
JOURNAL OF BIOSCIENCES, v.35, no.2, pp.241 - 248
Abstract
The antioxidant protein, adhesin thiol peroxidase (HpTpx or HP0390), plays an important role in enabling Helicobacter pylori to survive gastric oxidative stress. The bacterium colonizes the host stomach and produces gastric cancer. However, little information is available about the biochemical characteristics of HpTpx. We expressed recombinant HpTpx in Escherichia coli, purified to homogeneity, and characterized it. The results showed that HpTpx existed in a monomeric hydrodynamic form and the enzyme fully retained its peroxidase and antioxidant activities. The catalytic reaction of the enzyme was similar to an atypical 2-cysteine peroxiredoxin (Prx). The conformation of the enzyme was observed in the presence and absence of dithiothreitol (DTT); similar to other known thiol peroxidases, conformational change was observed in HpTpx by the addition of DTT.
Keywords
THIOREDOXIN PEROXIDASE; PEROXIREDOXIN; RESISTANCE; STRESS; SYSTEM; Adhesin thiol peroxidase; antioxidant protein; Circular dichroism; dithiothreitol; Helicobacter pylori; peroxiredoxin
ISSN
0250-5991
URI
https://pubs.kist.re.kr/handle/201004/131401
DOI
10.1007/s12038-010-0028-0
Appears in Collections:
KIST Article > 2010
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