Abstract:In this paper, it is first reported that Copper/Zinc Superoxide dismutase from Actinidia fruits has been isolated and purified and some properties have been studied. Purification by ammonium sulfate fractionation remove pectin, Sephadex G-100 gel filtration and DEAE-cellulose chromatorgraphy, 0.56mg CuZn-SOD with specific activity 1340 units per mg protein was obtained from 242g Actinidia fruits. The purified enzyme is found to be homogenous by the analysis of PAGE, SDS-PAGE, N-terminal aminoacid.SOD in the Actinidia fruits exhibits a absorption maximum in the ultravioiet at 270nm, and another in visible at 676nm. the enzyme Subunit molecular weight and molecular weight are 16800 and 33800 d. t. respectively. The subunit consists of approximate 157 amino acid residues, in which tryptophan residue is absent. The N-terminal amino acid is Ala as assayed by dansyl chloride, and replacement studies of the metal ions in the enzyme have been carried out using the metal Co and Zn.