E3289

Catalase from bovine liver

≥20000 units/mg protein, lyophilized powder

• Sinonimo/i: H₂O₂:H₂O₂ oxidoreductase
• Numero CAS: 9001-05-2
• NACRES: NA.54
• UNSPSC Code: 12352204
• EC Number: 232-577-1
• MDL number: MFCD00081483
• Numero CE: 1.11.1.6 (BRENDA, IUBMB)
• eCl@ss: 32160410
• Specific activity: ≥20000 units/mg protein

Proprietà

• form: lyophilized powder
• Quality Segment: 200
• specific activity: ≥20000 units/mg protein
• mol wt: tetramer ~250 kDa
• composition: protein, ≥60% E₄₀₅
• isoelectric point: 5.4
• shipped in: wet ice
• storage temp.: −20°C
• SMILES string: O(CC)C(=O)c1ccc(cc1)O
• 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

Descrizione

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 is encoded by the gene mapped to human chromosome 11p13. Mammalian catalase is an antioxidant enzyme and is a member of hydroperoxidase family). The active enzyme is homotetrameric in nature.

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

Catalase from bovine liver has been used:

• as a component of gloxy, which is one of the most popular oxygen-scavenging systems.
• in single molecule fluorescence resonance energy transfer (FRET) measurements.
• in cytochrome-C oxidase (COX) histochemistry to study the role of mitochondrial uncoupling protein 2 (UCP2) in limiting oxidative stress during glaucoma.
• to pre-treat slide chambers for total internal reflection fluorescence (TIRF) microscopy.[1]
• in quantifying hydrogen peroxide release.[2]
• to help minimize the effects of reactive oxygen species (ROS) in cooperativity assay for studying doublecortin and microtubule interaction.[3]

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.

Catalase has an ability to convert solar radiation into reactive oxidant species (ROS). It is involved in regulation of tissue peroxide levels. Mutation in catalase gene result in the progress of essential hypertension (EH).

Physical form

Supplied as a lyophilized powder containing ≤0.2% thymol

Other Notes

One unit will decompose 1.0 micromole of hydrogen peroxide per minute at pH 7.0 at 25 deg C, while the hydrogen peroxide concentration falls from 10.3 to 9.2 millimolar.

Informazioni sulla sicurezza

• pictograms: GHS08
• signalword: Danger
• hcodes: H334
• pcodes: P261 - P284 - P501
• Hazard Classifications: Resp. Sens. 1
• Classe di stoccaggio: 11 - Combustible Solids
• wgk: WGK 1
• flash_point_f: Not applicable
• flash_point_c: Not applicable