Nguyen, Huyen Thi Minh Nam, Kwang-Ho Saleem, Yasar Kim, Key-Sun 2024-01-20T19:04:18Z 2024-01-20T19:04:18Z 2021-09-02 2010-06 0250-5991 https://pubs.kist.re.kr/handle/201004/131401 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. English INDIAN ACAD SCIENCES Characterization of Helicobacter pylori adhesin thiol peroxidase (HP0390) purified from Escherichia coli Article 10.1007/s12038-010-0028-0 1 JOURNAL OF BIOSCIENCES, v.35, no.2, pp.241 - 248 JOURNAL OF BIOSCIENCES 35 2 241 248 N scie scopus 000278512100011 2-s2.0-78651270986 Biology Life Sciences & Biomedicine - Other Topics Article THIOREDOXIN PEROXIDASE PEROXIREDOXIN RESISTANCE STRESS SYSTEM Adhesin thiol peroxidase antioxidant protein Circular dichroism dithiothreitol Helicobacter pylori peroxiredoxin