18 products were found matching "S8060-09F.100"!

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Catalytic activity: 2 superoxide + 2 H+ = O2 + H2O2. COFACTOR: Binds 1 copper ion per subunit. Cofactor: Binds 1 zinc ion per subunit. Subunit: Homodimer. , Zinc binding promotes dimerization. Belongs to the...

Cu/Zn containing superoxide dismutase (SOD) belongs to the family of related enzymes which have the same catalytic function but are structurally different. SOD catalyzes the dismutation of the superoxide radical O2-to O2 and H2O2 which in turn is metabolized to H2O and O2 by catalase and glutathione peroxidase (1,...

Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2¯ to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2,5). In general, SODs play a...

Superoxide dismutase (SOD) is an enzyme, which thought to play a role in the protection of aerobic cells against oxygen toxicity by catalyzing disputation of superoxide anion (O2-) to H2O2 and O2. SODs are found in 3 forms and produced by separate genes. The first isoforms (SOD1, also known as SOD-A, soluble SOD,...

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Catalytic activity: 2 superoxide + 2 H+ = O2 + H2O2. COFACTOR: Binds 1 copper ion per subunit. Cofactor: Binds 1 zinc ion per subunit. Subunit: Homodimer. , Zinc binding promotes dimerization. Belongs to the...

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Catalytic activity: 2 superoxide + 2 H+ = O2 + H2O2. COFACTOR: Binds 1 copper ion per subunit. Cofactor: Binds 1 zinc ion per subunit. Subunit: Homodimer. , Zinc binding promotes dimerization. Belongs to the...

FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. CATALYTIC ACTIVITY: 2 superoxide + 2 H+ = O2 + H2O2. COFACTOR: Binds 1 copper ion per subunit. COFACTOR: Binds 1 zinc ion per subunit. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. DISEASE:...

Superoxide dismutase (SOD) is a 152aa enzyme previously known as haemocuprein or erythrocuprein and belongs to the Cu-Zn superoxide dismutase family. In mammals, it was first described in bovine erythrocytes and is a homodimeric non-covalently bound protein where each monomer has one intrachain disulphide and one...

Superoxide Dismutases (SODs), originally identified as Indophenoloxidase (IPO), are enzymes that catalyze the conversion of naturally-occuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 3, SOD3, also known as extracellular (EC) SOD, is tetrameric glycoprotein...

SOD3 is a member of the superoxide dismutase protein family. SODs are antioxidant enzymes that catalyse the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. SOD3 is thought to protect the brain, lungs and other tissues from oxidative stress. It is secreted into the extracellular space and...

Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2? to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play...

Superoxide Dismutases (SODs), originally identified as Indophenoloxidase (IPO), are enzymes that catalyze the conversion of naturally-occuring, but harmful, superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 3, SOD3, also known as extracellular (EC) SOD, is tetrameric glycoprotein...