Catalase from bovine liver contains 506 residues. It is a tetramer and each monomer corresponds to a molecular weight of 61 kDa. The active site in each momomer comprises nicotinamide adenine dinucleotide phosphate (NADPH) and iron binding region.

Research area: Cell Signaling

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.

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

Catalase from bovine liver has been used for measuring the hydrogen peroxide content in cancer tissue homogenates. It has also been used to test the effect of organophosphate insecticide chlorpyrifos-ethyl (CE) [0,0-diethyl 0 (3,5,6-trichloro-2-pyridyl) phosphorothioate] on its enzyme activity.

Catalase from bovine liver is used for the following applications:

• Dielectrophoretic field-flow fractionation (DEP-FFF): It is a chromatographic method in which cell elution times reflect the positions of cells in a hydrodynamic flow profile under the control of sedimentation, DEP and hydrodynamic lift forces, FSED, FDEP and FHDL, respectively. The DEP-FFF buffer consists of catalase along with other ingrediants.
• GC-MS analyses.
• Deionization.
• GC-FID analysis.5
• Functional analysis of blood vessel.

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.

This product doesn′t need any activators, but it is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogens bromide, 2-mercaptoethanol, dithiothreitol, dianisidnie and nitrate.

Solutions of catalse should not be frozen. Frozen solution will result in a 50-70% loss of activity.

One unit will decompose 1.0 μmole of H₂O₂ per min at pH 7.0 at 25 °C, while the H₂O₂ concentration falls from 10.3 to 9.2 mM, measured by the rate of decrease of A₂₄₀.

This product is a crystalline suspension in water containing 0.1% thymol with activity of 10,000-40,000 units/mg.

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