Some Properties of Cu, Zn-Superoxide Dismutase from Sheep Erythrocyte

Authors : Leman Tarhan

Pages : 109-116

View : 15 | Download : 8

Publication Date : 9999-12-31

Article Type : Makaleler

Abstract :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.
Keywords : Superoxide radical, Cu, Zn-superoxide dismutase, 6-hydroxydopamine, dismutation.