Characterization of Helicobacter pylori adhesin thiol peroxidase (HP0390) purified from Escherichia coli
- Characterization of Helicobacter pylori adhesin thiol peroxidase (HP0390) purified from Escherichia coli
- 뉴엔티민후옌; 남광호; 살림야사르; 김기선
- Adhesin thiol peroxidase; antioxidant protein; circular dichroism; dithiothreitol; Helicobacter pylori; peroxiredoxin
- Issue Date
- Journal of biosciences
- VOL 35, NO 2, 241-248
- 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.
- Appears in Collections:
- KIST Publication > Article
- Files in This Item:
There are no files associated with this item.
- RIS (EndNote)
- XLS (Excel)
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.