@article{oai:obihiro.repo.nii.ac.jp:00001018,
 author = {Masatani, Tatsunori and Asada, Masahito and Ichikawa-Seki, Madoka and Usui, Miho and Terkawi, Mohamad A. and Hayashi, Kei and Kawazu, Shin-ichiro and 河津, 信一郎 and Xuan, Xuenan and 玄, 学南},
 issue = {1},
 journal = {Journal of Veterinary Medical Science},
 month = {},
 note = {application/pdf, Peroxiredoxins (Prxs) are a family of antioxidant enzymes. Here, we cloned a 2-Cys Prx, BgTPx-1, from the canine Babesia parasite B. gibsoni. Sequence identity between BgTPx-1 and 2-Cys Prx of B. bovis was 81% at the amino acid level. Enzyme activity assay by using recombinant BgTPx-1 (rBgTPx-1) indicated that BgTPx-1 has antioxidant activity. Antiserum from a mouse immunized with rBgTPx-1 reacted with parasite lysates and detect a protein with a monomeric size of 22 kDa and also a 44 kDa protein, which might be an inefficiently reduced dimer. BgTPx-1 was expressed in the cytoplasm of B. gibsoni merozoites. These results suggest that the BgTPx-1 may play a role to control redox balance in the cytoplasm of B. gibsoni.},
 pages = {139--143},
 title = {Cloning and Characterization of a 2-Cys Peroxiredoxin from Babesia gibsoni},
 volume = {76},
 year = {2014}
}