EPR spectra of binuclear triazolato- and imidazolato-bridged copper(II) complexes including the four-copper form of bovine erythrocyte superoxide dismutase

1985 ◽  
Vol 24 (18) ◽  
pp. 2812-2815 ◽  
Author(s):  
A. Bencini ◽  
D. Gatteschi ◽  
C. Zanchini ◽  
J. G. Haasnoot ◽  
R. Prins ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Epr Spectra ◽  
Bovine Erythrocyte ◽  
Copper Form ◽  
Erythrocyte Superoxide Dismutase

ChemInform Abstract: EPR SPECTRA OF BINUCLEAR TRIAZOLATO- AND IMIDAZOLATO-BRIDGED COPPER(II) COMPLEXES INCLUDING THE FOUR-COPPER FORM OF BOVINE ERYTHROCYTE SUPEROXIDE DISMUTASE

1985 ◽  
Vol 16 (50) ◽  
Author(s):  
A. BENCINI ◽  
D. GATTESCHI ◽  
C. ZANCHINI ◽  
J. G. HAASNOOT ◽  
R. PRINS ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Epr Spectra ◽  
Bovine Erythrocyte ◽  
Copper Form ◽  
Erythrocyte Superoxide Dismutase

Anion binding to the four-copper form of bovine erythrocyte superoxide dismutase: mechanistic implications

Biochemistry ◽  
1981 ◽  
Vol 20 (26) ◽  
pp. 7488-7493 ◽  
Author(s):  
Kenneth G. Strothkamp ◽  
Stephen J. Lippard
Keyword(s):  
Superoxide Dismutase ◽  
Anion Binding ◽  
Bovine Erythrocyte ◽  
Copper Form ◽  
Erythrocyte Superoxide Dismutase

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

scholarly journals Anion Binding to Bovine Erythrocyte Superoxide Dismutase

1972 ◽  
Vol 247 (1) ◽  
pp. 60-65
Author(s):  
James A. Fee ◽  
Bruce P. Gaber
Keyword(s):  
Superoxide Dismutase ◽  
Anion Binding ◽  
Bovine Erythrocyte ◽  
Erythrocyte Superoxide Dismutase

Studies on the reconstitution of bovine erythrocyte superoxide dismutase

1973 ◽  
Vol 295 (1) ◽  
pp. 96-106 ◽  
Author(s):  
James A. Fee ◽  
Ray Natter ◽  
George S.T. Baker
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.

Voltammetric behaviour of bovine erythrocyte superoxide dismutase

1992 ◽  
Vol 27 (2) ◽  
pp. 229-233 ◽  
Author(s):  
M. Borsari ◽  
H.A. Azab
Keyword(s):  
Superoxide Dismutase ◽  
Bovine Erythrocyte ◽  
Erythrocyte Superoxide Dismutase
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