Superoxide dismutase (SOD) was isolated from sheep erythrocyte. SOD activity was measured under the optimized assay conditions by observing the variations of autoxidation rate of 6-hydroxydopamine (6-OHDA). The enzyme was characterized as containing copper and zinc and was insensitive to chloroform-ethanol mixture but inhibited by cyanide and hydrogen peroxide. The activity variations and stability properties of sheep erythrocyte Cu, Zn-SOD were investigated under the optimized activity assay conditions by observing inhibition change at the autoxidation rate of 6-OHDA. The optimum pH and temperature of sheep erythrocyte Cu, Zn-SOD were found to be 9.4 and 30\circC respectively. The enzyme showed high pH- and thermal-stability properties around neutral pH and up to 37\circC after 2.5 h incubation. Variations in the inhibition percentage of autoxidation were investigated in 0.2-0.9 mM range of 6-OHDA. The same procedures were repeated by adding catalase also.

Superoxide dismutase (SOD) was isolated from sheep erythrocyte. SOD activity was measured under the optimized assay conditions by observing the variations of autoxidation rate of 6-hydroxydopamine (6-OHDA). The enzyme was characterized as containing copper and zinc and was insensitive to chloroform-ethanol mixture but inhibited by cyanide and hydrogen peroxide. The activity variations and stability properties of sheep erythrocyte Cu, Zn-SOD were investigated under the optimized activity assay conditions by observing inhibition change at the autoxidation rate of 6-OHDA. The optimum pH and temperature of sheep erythrocyte Cu, Zn-SOD were found to be 9.4 and 30\circC respectively. The enzyme showed high pH- and thermal-stability properties around neutral pH and up to 37\circC after 2.5 h incubation. Variations in the inhibition percentage of autoxidation were investigated in 0.2-0.9 mM range of 6-OHDA. The same procedures were repeated by adding catalase also.