Isolation and Properties of Superoxide Dismutase from Bovine Spermatozoa1

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Abstract
Two forms of superoxide dismutase were discerned in sonicated bovine spermatozoa. One form was 76,000-77,000 daltons and cyanide-insensitive, properties characteristic of the manganosuperoxide dismutase. The other, 33,000-34,000 daltons, was cyanide-sensitive and corresponded to the copper-zinc enzyme described in ram spermatozoa. Total activity for both types of superoxide dismutase was 41 units/109 spermatozoa. The low MW enzyme was purified to homogeneity as evidenced by sodium dodecyl sulfate polyacrylamide gel electrophoresis. It exhibited the properties characteristic of copper-zinc superoxide dismutase isolated from other bovine tissues. Owing to instability, the high MW form of the enzyme could not be similarly purified.