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2 O2.- + 2 H+ +
O2 + H2O2
2 superoxide + 2 H+
O2 + H2O2
nitro blue tetrazolium + ?
?
Nitroblue Tetrazolium + ?
?
O2.- + 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate
?
i.e. WST-1, activity assay detection method
-
-
?
additional information
?
-
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
activity determination by the epinephrine assay: at alkaline pH, superoxide anion O2- causes the oxidation of epinephrine to adrenochrome, SOD competes with this reaction by decreasing the adrenochrome formation
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
ir
2 O2.- + 2 H+
O2 + H2O2
-
enzyme activity determination by xanthine-xanthine oxidase-nitro blue tetrazolium assay
-
-
ir
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
enzyme activity assay by measurement of inhibition of reduction of cytochrome c by O2- produced by the xanthine oxidase/xanthine reaction
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
superoxide dismutase is a key enzyme for the protection of aerobic organisms against toxic radicals produced during oxidative processes
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
dismutation of superoxide in a two-step reaction: 1. O2.- + Fe3+-SOD = O2 + Fe2+-SOD, 2. O2.- + Fe2+-SOD + 2 H+ = H2O2 + Fe3+-SOD
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
Thermochaetoides thermophila
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
detoxification of superoxide
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
Photobacterium sepia
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
nitro blue tetrazolium + ?
?
-
-
-
-
?
nitro blue tetrazolium + ?
?
-
-
-
-
?
Nitroblue Tetrazolium + ?
?
-
enzyme inhibits superoxide-induced reduction of colorless Nitroblue Tetrazolium dye to its oxidized blue formazan form
-
-
?
Nitroblue Tetrazolium + ?
?
-
enzyme inhibits superoxide-induced reduction of colorless Nitroblue Tetrazolium dye to its oxidized blue formazan form
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Anas platyrhynchos domestica CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Mn-SOD, expression is strongly stimulated during stationary phase in cell culture, enzyme is atypical and plays an important role in cell protection against reactive oxygen in the cytosol in the stationary phase
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Megalodesulfovibrio gigas
-
-
-
?
O2- + H+
O2 + H2O2
Megalodesulfovibrio gigas Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Radix lethospermi
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
a metalloenzyme that eliminates superoxide radicals by dismutation into hydrogen peroxide and molecular oxygen
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
Deinococcus radiodurans Mn-SOD is most effective at high superoxide fluxes found under conditions of high radioactivity compared to te enzyme of Escherichia coli and Homo sapiens
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
a key enzyme for fighting oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments, thereby preventing activation of polymorphic neutrophil chemotaxis by fragmented hyaluronic acid, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme mutation E93A leads to a decrease in muscle cdk5 activity accompanied by a significant reduction in MyoD and cyclin D1 levels causing amyotrophic lateral sclerosis, a primarily a motor neuron disorder with early muscle denervation preceding motor neuron loss, the progressive deterioration of muscle function is potentiated by altered muscle biochemistry in these mice at a very young, presymptomatic age, overview
-
-
?
O2.- + H+
O2 + H2O2
the conserved, active-site residue Tyr34 mediates product inhibition
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid via its matrix-binding domain and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments
-
-
?
O2.- + H+
O2 + H2O2
-
enzyme inhibition by tetrathiomolybdate leads to antiangiogenic and antitumour effects in mice
-
-
?
O2.- + H+
O2 + H2O2
-
rosuvastatin induces the enzyme in aortic extracts and restores the enzyme expression in mice with combined leptin and LDL-receptor deficiency, and in THP-1 macrophages and foam cells in vitro, thus, SOD1 is a potentially important mediator of the prevention of oxLDL accumulation within atherosclerotic plaques, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
extracellular superoxide dismutase accelerates endothelial recovery and inhibits in-stent restenosis in stented atherosclerotic Watanabe heritable hyperlipidemic rabbit aorta. Extracellular superoxide dismutase, EC-SOD, is a major component of antioxidative defense in blood vessels, and exogenously delivered EC-SOD protects against balloon-induced neointima formation and constrictive remodeling and has powerful cardioprotective properties, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme is important in defense of cells against oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
Cu,ZnSOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
-
-
?
O2.- + H+
O2 + H2O2
-
SOD1 induces Ca2+ in the cell and inhibits ERK phosphorylation in the P-ERK1/2 pathway by muscarinic receptor M1 modulation in rat pituitary GH3 cells, the effect is enhanced by oxotremorine and partially reverted by pyrenzepine, and independent from increased intracellular calcium concentration, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme is involved in hypoxic pulmonary vasoconstriction, HPV, an important physiological mechanism, which is regulated by changes in the production of and interactions among reactive oxygen species, mechanism, overview, the superoxide dismutase mimetic tempol inhibits HPV, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme prevents the inhibition of human CYP3A4, UGT1A6, and P-glycoprotein with halogenated xanthene food dyes, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
the enzyme contributes to the virulence of many human-pathogenic fungi through its ability to neutralize toxic levels of reactive oxygen species generated by the host
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
pyrogallol + ?
?
-
-
-
?
pyrogallol + ?
?
enzyme inhibits the autooxidation of pyrogallol
-
-
?
pyrogallol + ?
?
-
enzyme inhibits the autooxidation of pyrogallol
-
-
?
riboflavin + ?
?
-
-
-
-
?
riboflavin + ?
?
-
-
-
-
?
additional information
?
-
SOD activity is determined by a modified method of inhibition of cytochrome c reduction in a xanthine/xanthine oxidase system generating superoxide ions
-
-
?
additional information
?
-
-
SOD activity is determined by a modified method of inhibition of cytochrome c reduction in a xanthine/xanthine oxidase system generating superoxide ions
-
-
?
additional information
?
-
-
SOD enzyme activity is determined by measuring enzyme ability to inhibit the photochemical reduction of nitrobluetetrazolium
-
-
?
additional information
?
-
-
the enzyme is involved in activation and modulation of phospho-extracellular signal-regulated kinases proteins and in the control of several biological processes including cell proliferation
-
-
?
additional information
?
-
-
SOD activity measurement using the nitroblue tetrazolium
-
-
?
additional information
?
-
-
SOD activity measurement using the nitroblue tetrazolium
-
-
?
additional information
?
-
-
enzyme activity measurement by determination of inhibition through the enzyme of pyrogallol autoxidation to purpurogallin
-
-
?
additional information
?
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enzyme can reduce ferrocyanide to ferricyanide at pH 5.0-8.7
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addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I)
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SOD inhibits the autoxidation of pyrogallol
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coupled assay method using inhibition of the autooxidation of pyrogallol
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superoxide dismutase inhibits pyrogallol autoxidation in alkaline medium characterized by increases in oxygen consumption. The primary products of pyrogallol autoxidation are H2O2 by reduction of O2 and pyrogallol-orthoquinone by oxidation of pyrogallol. SOD is catalyzing a reaction that annuls the forward electron transfer step that produces superoxide and pyrogallol-semiquinone, both oxygen radicals. By dismutating these oxygen radicals, SOD can reverse autoxidation. Analysis of reaction parameters, overview
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enzyme can reduce ferrocyanide to ferricyanide at pH 5.0-8.7
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additional information
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addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I)
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additional information
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enzyme activity assay method using riboflavin and nitroblue tetrazolium (NBT) reduction
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SOD activity is assayed based on its ability to compete with nitroblue-tetrazolium for superoxide anions generated by the xanthine-xanthine oxidase system, which in turn results in the inhibition of reduction of nitroblue-tetrazolium
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SOD activity is assayed based on its ability to compete with nitroblue-tetrazolium for superoxide anions generated by the xanthine-xanthine oxidase system, which in turn results in the inhibition of reduction of nitroblue-tetrazolium
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Cu,Zn-dependent enzyme protects photoheterotrophic cells from periplasmic superoxide generated by exposure to low O2 under illuminated conditions
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SOD activity measurement by the ferricytochrome c method, using xanthine/xanthine oxidase as the source of superoxide radicals
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the extracellular enzyme appears to bind lipopolysaccharides, recognition mechanisms can be provided by several actors which can interplay such as plasma LBP-binding protein (LBP), membrane bound or soluble forms of CD14 and integrins
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enzyme Sod2 is a major component of the antioxidant defense system, and adaptation to elevated growth temperatures is also dependent on enzyme activity
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the enzyme activity assay uses the p-nitro blue tetrazolium chloride (NBT) solution method
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the enzyme activity assay uses the p-nitro blue tetrazolium chloride (NBT) solution method
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equilibrium binding of Escherichia coli MnSOD to poly(U), poly(A), poly(C), poly(dU) and double-stranded (ds) DNA, overview. The polynucleotides bind to MnSOD in the following affinity hierarchy, poly(dU) N poly(U) N dsDNA N poly(A) N poly(C). The differences in the hierarchy are not large in magnitude as the poly(dU) bound with less than a 100fold higher affinity than poly(C). For each polynucleotide, Kobs decreases only slightly with increasing [K+], surprising for a relatively non-specific nucleic acid protein. There is either only one binding site shared by these polynucleotides or the larger site size occluded by poly(C) overlaps that of poly(U) and poly(A), but extends further on the protein
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enzyme activity assay using nitroblue tetrazolium and riboflavin
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determination of superoxide dismutase is performed using the method of inhibition of epinephrine auto-oxidation in alkaline medium and the measurement of the absorbance of the resulting product at 340 nm
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EC-SOD protects the lung in both bleomycin- and asbestos-induced models of pulmonary fibrosis
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pharmacokinetics of single and multiple doses of recombinant human superoxide dismutase covalently linked to lecithin in healthy Japanese and Caucasian volunteers are nonlinear with dose, showing a relatively long half-life of PC-SOD of over 24 hours, overview
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pharmacokinetics, safety and tolerability of single rising doses up to 80 mg of recombinant human superoxide dismutase covalently linked to lecithin in healthy white volunteers, overview
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enzyme activity detection by water-soluble tetrazolium (WST-1) assay. This assay is based on the detection of a water-soluble formazan dye that is formed upon reduction of water-soluble tetrazolium salt, WST-1, by the superoxide anion
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additional information
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enzyme activity detection by water-soluble tetrazolium (WST-1) assay. This assay is based on the detection of a water-soluble formazan dye that is formed upon reduction of water-soluble tetrazolium salt, WST-1, by the superoxide anion
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the enzyme activity is detected by its ability to inhibit the autoxidation of epinephrine at pH 10.2
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the enzyme activity is detected by its ability to inhibit the autoxidation of epinephrine at pH 10.2
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SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
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SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
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additional information
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SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
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additional information
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SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
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the enzyme assay measures the enzyme's ability to inhibit the oxidation of hydroxylamine catalyzed by the xanthine-xanthine oxidase system
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the enzyme assay measures the enzyme's ability to inhibit the oxidation of hydroxylamine catalyzed by the xanthine-xanthine oxidase system
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enzyme activity of recombinant MgMnSOD1 is assayed by using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium, i.e. WST-1. The method shows high sensitivity due to the lower reaction rate of WST-1 and superoxide anion
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enzyme activity of recombinant MgMnSOD1 is assayed by using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium, i.e. WST-1. The method shows high sensitivity due to the lower reaction rate of WST-1 and superoxide anion
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inverse relationship between SOD1 expression and ox-LDL in plaque plays a role in oxidative stress contributes to post-ischaemic injury in the heart, increasing SOD1 protects against this increased oxidative stress
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enzyme is involved in pathogenesis of the parasite by protecting it from oxidative killing
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higher levels of oxidative stress may induce changes in photochemicla efficiency of photosystem II
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enzyme PschSOD exhibits superoxide dismutase and peroxidase activities. The enzyme utilizes its own dismutation product, the H2O2 in presence of bicarbonate
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enzyme PschSOD exhibits superoxide dismutase and peroxidase activities. The enzyme utilizes its own dismutation product, the H2O2 in presence of bicarbonate
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the enzyme is required for virulence of the organism, e.g. in silkworm Bombyx mori, with iron-SOD being more important, overview
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superoxide dismutase activity in Pseudomonas putida affects utilization of sugars and growth on root surfaces, role of SOD in root colonization and oxidative stress, overview
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dismutation of superoxide anions is promoted by reduction of Cu2+ to Cu+
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MnSOD may have a specific role in the steroidogenic function of the fasciulata/reticularis of the rat adrenal, but not on that of the glomerulosa
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dismutation of superoxide anions is promoted by reduction of Cu2+ to Cu+
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enzyme activity measurement by reduction of NBT
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enzyme activity measurement by reduction of NBT
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additional information
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enzyme activity measurement by reduction of NBT
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covalent modification of the conserved Tyr41 in the active site, Tyr41 and His155 are involved in catalysis, hydrogen bond network including three solvent molecules connecting the iron-ligating hydroxide ion via H155 with F41 and H37, Y41 and H155 are important for the structural and functional properties of SOD, overview
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native and recombinant enzyme ossess a covalent modification of the conserved Tyr41 in the active site, Tyr41 plays an important role in the enzyme activity and the maintenance of the structural architecture of SOD, overview
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native and recombinant enzyme ossess a covalent modification of the conserved Tyr41 in the active site, Tyr41 plays an important role in the enzyme activity and the maintenance of the structural architecture of SOD, overview
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unusual covalent modification of the conserved Tyr41 in the active site, interactions Tyr41-His155, overview
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SOD activity is measured using a method employing xanthine and xanthine oxidase to generate superoxide radicals which react with 2-(4-iodophenyl)-3-(4-nitrophenol)-5-phenyltetrazolium chloride (INT) to form a red formazan dye. The SOD activity is then measured spectrophotometrically by the degree of inhibition of this reaction by means of the decrease in absorbance at 505 nm, 37°C
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enzyme activity is measured byy the enzyme caused inhibition of the xanthine oxidase coupling reaction
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enzyme activity determination with riboflavin and nitroblue tetrazolium (NBT), kinetics
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Fe2+-containing active site structure, overview
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Fe2+-containing active site structure, overview
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SOD enzyme activity measurement is based on the inhibition of nitroblue tetrazolium reduction by superoxide radical generated by xanthine/xanthine oxidase
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additional information
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superoxide dismutase activity is measured by the inhibition of nitro blue tetrazolium reduction in the presence of the superoxide anion generated by the xanthine and xanthine oxidase system
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additional information
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enzyme activity determination by NBT reduction
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the enzyme activity is determined by measuring by inhibition of autooxidation of pyrogallol
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