| dc.creator |
Tarhan, L |
|
| dc.creator |
Tuzmen, MN |
|
| dc.date |
2000-01-01T01:00:00Z |
|
| dc.date.accessioned |
2021-12-03T11:31:40Z |
|
| dc.date.available |
2021-12-03T11:31:40Z |
|
| dc.identifier |
87a411a9-af07-4ecc-a4ba-b49eb2c934a7 |
|
| dc.identifier |
https://avesis.sdu.edu.tr/publication/details/87a411a9-af07-4ecc-a4ba-b49eb2c934a7/oai |
|
| dc.identifier.uri |
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/93135 |
|
| dc.description |
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 degrees C respectively. The enzyme showed high pH- and thermal-stability properties around neutral pH and up to 37 degrees C 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. |
|
| dc.language |
eng |
|
| dc.rights |
info:eu-repo/semantics/closedAccess |
|
| dc.title |
Some properties of Cu, Zn-superoxide dismutase from sheep erythrocyte |
|
| dc.type |
info:eu-repo/semantics/article |
|