C3155

Catalase from bovine liver

aqueous solution, ≥30,000 units/mg protein

• Synonym(s): H₂O₂:H₂O₂ oxidoreductase
• CAS Number: 9001-05-2
• Enzyme Commission number: 1.11.1.6 (BRENDA, IUBMB)
• MDL number: MFCD00081483
• UNSPSC Code: 12352200
• NACRES: NA.32

Properties

• biological source: bovine liver
• Quality Level: 200
• description: optimum pH ~ 7.0
• sterility: aseptically filled
• form: aqueous solution
• specific activity: ≥30,000 units/mg protein
• mol wt: tetramer ~250 kDa
• contains: ≤0.10 mg/mL Thymol
• composition: ammonium sulphate, 30-50% ; catalase, 10-20%
• storage condition: (Tightly closed. Keep locked up or in an area accessible only to qualified or authorized; persons)
• technique(s): activity assay: suitable
• isoelectric point: 5.4
• pI: 5.4
• UniProt accession no.: P00432
• shipped in: wet ice
• storage temp.: 2-8°C
• InChI: 1S/C9H10O3/c1-2-12-9(11)7-3-5-8(10)6-4-7/h3-6,10H,2H2,1H3
• InChI key: NUVBSKCKDOMJSU-UHFFFAOYSA-N
• Gene Information: cow ... CAT(280743)

Description

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.

Research area: Cell Signaling

Catalase from bovine is a tetrameric enzyme, consisting of four identical sub-units containing a single heme moiety per subunit. Each subunit has four domains like the α-helical domain, an eight-stranded β-barrel, N-terminal threading arm that is connected to the β-barrel via a wrapping loop.

Application

Catalase from bovine liver has been used:

• as a component of the GLOX buffer during single molecule fluorescent in situ hybridization (smFISH) on primary mouse cortical neurons
• for its structural and kinetic analysis of its interaction with nitric oxide
• in the preparation of glucose oxidase-catalase system (GOX-CAT system) to generate H2O2 and study the effect of H2O2-induced oxidative stress on myelination in mouse organotypic cerebellar slice cultures

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 is an active, ubiquitous enzyme that is found in all aerobic organisms. Lower levels of catalase and oxidative stress lead to several disorders such as vitiligo, hypertension, acatalasemia, cancer, diabetes mellitus, and Alzheimer’s.

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.

Caution

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

Unit Definition

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.

Preparation Note

This product is an aqueous solution containing >30,000 units/mg protein. To remove the thymol preservative, the catalase crystals may be pelleted by centrifugation, the supernatant, discarded, the pellet resuspended in water, and then pelleted again. The enzyme is soluble in 50 mM potassium phosphate buffer at 1 mg/mL and pH 7.0.

Safety Information

• Pictograms: GHS08
• Signal Word: Danger
• Hazard Statements: H334
• Precautionary Statements: P261 - P284 - P501
• Hazard Classifications: Resp. Sens. 1
• Storage Class Code: 12 - Non Combustible Liquids
• WGK: WGK 1
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable
• Personal Protective Equipment: dust mask type N95 (US), Eyeshields, Gloves