Cytosol fraction was isolated from Fasciola hepatica and cytosolic Cu, Zn- superoxide dismutase (EC 1.15.1.1, SOD) was purified by ammonium sulfate precipitation, DEAE-Trisacryl M column chromatography and Sephadex G-100 gel filtration, and some physical properties of the purified enzyme was observed.
The results were summarized as follows:
1. The cytosolic Cu, Zn-SOD was purified approximately 255 fold..
2. The molecular weight of purified enzyme was estimated to be 34Kd by Sephadex G-100 gel filtration, and 17Kd by SDS-PAGE and so, it was composed of two subunits of equal size, which were not rovalently ,joined.
3. The purified enzyme was observed 3.5 times more active when the buffer pH raised to 10.0.
4. The activity of purified enzyme was inhibited 100´lo by 1mM cyanide.
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