Formate as an NMR probe of anion binding to copper-zinc and copper-cobalt bovine erythrocyte superoxide dismutase

Biochemistry ◽  
1992 ◽  
Vol 31 (49) ◽  
pp. 12410-12415 ◽  
Author(s):  
Marco Sette ◽  
Maurizio Paci ◽  
Alessandro Desideri ◽  
Giuseppe Rotilio
Keyword(s):  
Superoxide Dismutase ◽  
Anion Binding ◽  
Bovine Erythrocyte ◽  
Erythrocyte Superoxide Dismutase ◽  
Copper Zinc

scholarly journals Bovine Erythrocyte Superoxide Dismutase

1974 ◽  
Vol 249 (22) ◽  
pp. 7339-7347
Author(s):  
John L. Abernethy ◽  
Howard M. Steinman ◽  
Robert L. Hill
Keyword(s):  
Superoxide Dismutase ◽  
Bovine Erythrocyte ◽  
Erythrocyte Superoxide Dismutase

A KINETIC STUDY OF REDUCTION OF BOVINE ERYTHROCYTE SUPEROXIDE DISMUTASE WITH POTASSIUM HEXACYANOFERRATE(II)

1983 ◽  
Vol 12 (9) ◽  
pp. 1429-1432 ◽  
Author(s):  
Junzo Hirose ◽  
Mayumi Ueoka ◽  
Tamami Tsuchiya ◽  
Mikiko Nakagawa ◽  
Masahide Noji ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Kinetic Study ◽  
Potassium Hexacyanoferrate ◽  
Bovine Erythrocyte ◽  
Erythrocyte Superoxide Dismutase

Superoxide Dismutase Activity in Bovine Milk Serum

1979 ◽  
Vol 42 (11) ◽  
pp. 867-871 ◽  
Author(s):  
M. KORYCKA-DAHL ◽  
T. RICHARDSON ◽  
C. L. HICKS
Keyword(s):  
Superoxide Dismutase ◽  
Cytochrome C ◽  
Polyacrylamide Gel Electrophoresis ◽  
Bovine Milk ◽  
Enzymic Activity ◽  
Superoxide Dismutase Activity ◽  
Bovine Erythrocyte ◽  
Milk Serum ◽  
Erythrocyte Superoxide Dismutase ◽  
Acid Whey

Superoxide dismutase activity was shown to be present in bovine milk serum and was quantified by measuring the capacity of retentate from dialyzed milk serum to inhibit reduction of cytochrome c by xanthine-xanthine oxidase-generated superoxide anion. One unit of enzyme was defined as the quantity of superoxide dismutase which inhibits cytochrome c reduction by 20%. By this definition 19,500 units of enzyme were present per liter of retentate from dialyzed milk serum. This amount is equivalent to about 2.4 mg of purified bovine erythrocyte superoxide dismutase per liter. Polyacrylamide gel electrophoresis of a partially-purified superoxide dismutase from acid whey, followed by staining for enzymic activity, confirmed the presence of the enzyme in milk serum which was identical in electrophoretic properties to those of bovine erythrocyte copper-zinc superoxide dismutase. Pasteurization at 63 C for 30 min did not decrease superoxide dismutase activity in milk serum. Heating of purified bovine erythrocyte-superoxide dismutase at 100 C for 1 min resulted in almost complete loss of enzymic activity, whereas the partially-purified superoxide dismutase from acid whey still retained 40% of the original activity under these conditions. Bovine milk superoxide dismutase may be an important naturally-occurring antioxidant for increasing oxidative stability of milk and other dairy products.

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