Identification and characterization of a mitochondrial iron-superoxide dismutase of Cryptosporidium parvum
- Authors
- Kang, Jung-Mi; Cheun, Hyeng-Il; Kim, Juri; Moon, Sung-Ung; Park, Soon-Jung; Kim, Tong-Soo; Sohn, Woon-Mok; Na, Byoung-Kuk
- Issue Date
- Sep-2008
- Publisher
- SPRINGER
- Citation
- PARASITOLOGY RESEARCH, v.103, no.4, pp.787 - 795
- Indexed
- SCIE
SCOPUS
- Journal Title
- PARASITOLOGY RESEARCH
- Volume
- 103
- Number
- 4
- Start Page
- 787
- End Page
- 795
- URI
- https://scholarworks.bwise.kr/gnu/handle/sw.gnu/27274
- DOI
- 10.1007/s00436-008-1041-1
- ISSN
- 0932-0113
- Abstract
- Cryptosporidium parvum is an intracellular protozoan parasite that causes cryptosporidiosis in mammals. In this study, we identified a gene encoding mitochondrial iron-superoxide dismutase of C. parvum (Cp-mtSOD) and characterized biochemical properties of the recombinant protein. Multiple sequence alignment of the deduced amino acid sequence of Cp-mtSOD with those of previously reported iron-containing SODs (Fe-SODs) from other protozoan parasites showed that Cp-mtSOD shares common metal-binding residues and motifs that were conserved in Fe-SODs. However, the N-terminal 26-amino acid residues of Cp-mtSOD did not show sequence identities to any other Fe-SOD sequences. Further analysis of the N-terminal presequence of Cp-mtSOD suggested that it shares common physiochemical characteristics found in mitochondria targeting sequences and predicted localization of Cp-mtSOD in the mitochondria. The recombinant Cp-mtSOD showed typical biochemical properties with other characterized Fe-SODs, including molecular structure, broad pH optimum, and sensitivity to hydrogen peroxide.
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