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.
Functional Expression of a Recombinant Copper/Zinc Superoxide Dismutase of Filarial Nematode, Brugia malayi
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W-G. Lee, J-H. Hwang, B-K. Na, J-H. Cho, H-W. Lee, S-H. Cho, Y. Kong, C-Y. Song, T-S. Kim; Functional Expression of a Recombinant Copper/Zinc Superoxide Dismutase of Filarial Nematode, Brugia malayi. J Parasitol 1 February 2005; 91 (1): 205–208. doi: https://doi.org/10.1645/GE-285R
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