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

Title
Characterization of Helicobacter pylori adhesin thiol peroxidase (HP0390) purified from Escherichia coli
Authors
뉴엔티민후옌남광호살림야사르김기선
Keywords
Adhesin thiol peroxidase; antioxidant protein; circular dichroism; dithiothreitol; Helicobacter pylori; peroxiredoxin
Issue Date
2010-06
Publisher
Journal of biosciences
Citation
VOL 35, NO 2, 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, purifi ed 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.
URI
http://pubs.kist.re.kr/handle/201004/38231
ISSN
0250-5991
Appears in Collections:
KIST Publication > Article
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