Articles
STUDY ON SUPEROXIDE DISMUTASE IN SATUREJA HORTENSIS L. ROOTS
Article number
723_26
Pages
215 – 220
Language
English
Abstract
In this research we investigated the superoxide dismutase (SOD) activity in Satureja hortensis roots.
Only 1 ± 0.2 units enzyme per mg protein were detectable by the method involving nitro blue tetrazolium reduction, while 30 ± 2 and 57 ± 6 units per mg protein were detectable by the methods involving respectively cytochrome c reduction and pyrogallol autooxidation.
The latter was thus the most suitable method for detecting SOD activity in the extract.
Root extracts were also subjected to electrophoresis in nondenaturing polyacrylamide gel followed by activity staining for SOD. Five bands were detectable that were attributed to copper/zinc- and manganese-SOD, based on their differential sensitivity to cyanide and hydrogen peroxide; no iron-SOD was detectable.
Only 1 ± 0.2 units enzyme per mg protein were detectable by the method involving nitro blue tetrazolium reduction, while 30 ± 2 and 57 ± 6 units per mg protein were detectable by the methods involving respectively cytochrome c reduction and pyrogallol autooxidation.
The latter was thus the most suitable method for detecting SOD activity in the extract.
Root extracts were also subjected to electrophoresis in nondenaturing polyacrylamide gel followed by activity staining for SOD. Five bands were detectable that were attributed to copper/zinc- and manganese-SOD, based on their differential sensitivity to cyanide and hydrogen peroxide; no iron-SOD was detectable.
Publication
Authors
F. Attar, N. Einollahi, E. Keyhani, J. Keyhani
Keywords
Enzymatic activity gel electrophoresis
Online Articles (69)