[Purification and comparative study of superoxide dismutase from animal tissues].

Cuprozinc superoxide dismutases were isolated from bovine liver, kidney and adrenal medulla. It was found that the enzyme from these sources exists in the form of three isoenzymes, the main izoenzyme being the most basic form. Physico-chemical properties of superoxide dismutases isolated from different tissues were found similar. Copper atoms in active sites of all superoxide dismutases investigated are bound with 4 nitrogen atoms.