Merck, SRE0041-10G, Catalase from bovine liver

General description
Research Area: Cell Signaling

Catalase from bovine liver is a tetramer consisting of 4 equal subunits each with a 60 kDa molecular weight. Each of these subunits contains iron bound to a protoheme IX group. The enzyme will also strongly bind to NADP, where NADP and the heme group are within 13.7 angstroms.
Application
Catalase acts as a natural antioxidant to study the roles of reactive oxygen species in gene expression and apoptosis. It has also been used to protect against oxidative damage to proteins, lipids, and nucleic acids. Industrially, catalzes have been used to remove hydrogen peroxide added to milk and cheese, in textile bleaching, and to examine its positive effects on the viability of DNA-repair mutants of E. coli.

Catalase from bovine liver may be used:

to prepare H₂O₂-O₂ based biocathode for applications in glucose biofuel cells
to study the kinetic properties and storage stability of catalase immobilized on to florisil
in glutathione-mediated superoxide generation in an aqueous solution

Biochem/physiol Actions
Catalase, an antioxidant enzyme found in all aerobic organisms, catalyzes the degradation of hydrogen peroxide, a byproduct of metabolic processes, into less harmful water and oxygen. It can also react with alkylhydrogen peroxides, such as methylperoxide and ethylperoxide and the second H₂O₂ molecule can be replaced by methanol, ethanol, propanol, formate and nitrate as a hydrogen donor. Catalase enzyme uses either iron (Fe) or manganese (Mn) as cofactor, and are classified as Fe-CAT or Mn-CAT.
Other Notes
One unit will decompose 1.0 micromole of hydrogen peroxide per minute at pH 7.0 and 25 deg C, while the hydrogen peroxide concentration falls from 10.3 to 9.2 millimolar.