Functional expression of a recombinant copper/zinc superoxide dismutase of filarial nematode, Brugia malayi
Journal of Parasitology, ISSN: 0022-3395, Vol: 91, Issue: 1, Page: 205-208
2005
- 5Citations
- 8Captures
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Metrics Details
- Citations5
- Citation Indexes5
- CrossRef4
- Captures8
- Readers8
Article Description
A gene encoding a copper/zinc superoxide dismutase (Cu/ Zn-SOD) of a filarial nematode, Brugia malayi, has been isolated and the biochemical properties of a functionally expressed recombinant enzyme were investigated. The cloned complementary DNA contained a single open reading frame of 477 bp encoding 158 amino acids (aa), which conserved metal-binding residues as well as residues specific for Cu/Zn-SODs. Comparison of the deduced aa sequence of the enzyme with that of other helminthes species, including filarial worms, exhibited high degree of similarities (49-98%). Recombinant enzyme of 32 kDa had an isoelectric point of 6.6 and was shown to consist of 2 subunits linked by interchain disulfide bonds. Enzyme activity of the recombinant protein was inhibited by potassium cyanide and hydrogen peroxide but not by sodium azide. It showed a wide range of pH optima, i.e., 7.0-11.0 and was highly resistant to heat inactivation. © American Society of Parasitologists 2005.
Bibliographic Details
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