Superoxide dismutase (SOD) catalyzes the removal of the O2- free radical. The enzyme protects oxygen-metabolizing cells against harmful effects of superoxide free-radicals. Superoxide dismutase is inactivated by H2O2. It consists of two subunits of identical molecular weight joined by a disulfide bond. The molecular weight is 32,500 daltons, and there are two Cu(II) and two Zn(II) atoms per molecule. The isoelectric point of the enzyme is 4.95.Superoxide dismutase from bovine erythrocytes has been used in a study to assess a kinetic model of radiation-induced inactivation of superoxide dismutase in nitrous oxide-saturated solutions. Superoxide dismutase from bovine erythrocytes has also been used in a study to investigate the possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction.
Superoxide dismutase (SOD) catalyzes the removal of the O2- free radical. The enzyme protects oxygen-metabolizing cells against harmful effects of superoxide free-radicals. Superoxide dismutase is inactivated by H2O2. It consists of two subunits of identical molecular weight joined by a disulfide bond. The molecular weight is 32,500 daltons, and there are two Cu(II) and two Zn(II) atoms per molecule. The isoelectric point of the enzyme is 4.95.
Superoxide dismutase from bovine erythrocytes has been used in a study to assess a kinetic model of radiation-induced inactivation of superoxide dismutase in nitrous oxide-saturated solutions. Superoxide dismutase from bovine erythrocytes has also been used in a study to investigate the possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction.
L2318235
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