Superoxide Dismutase from Lens esculenta

Abstract
Superoxide dismutase was purified to homogeneity from L. esculenta cotyledons and shoots. The 2 forms appeared identical. The purified enzyme contained 2 electrophoretically distinct bands. It contained 2 ions of Cu and 2 ions of Zn. Gel filtration experiments indicate a MW of about 33,000. The spectrum of UV and visible regions and EPR were similar to those of Cu-Zn mammalian superoxide dismutase.

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