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C3155

Sigma-Aldrich

Catalase from bovine liver

aqueous solution, ≥30,000 units/mg protein

Synonyme(s) :

H2O2:H2O2 oxidoreductase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

bovine liver

Niveau de qualité

Description

optimum pH ~ 7.0

Stérilité

aseptically filled

Forme

aqueous solution

Activité spécifique

≥30,000 units/mg protein

Poids mol.

tetramer ~250 kDa

Contient

≤0.10 mg/mL Thymol

Composition

ammonium sulphate, 30-50%
catalase, 10-20%

Conditions de stockage

(Tightly closed. Keep locked up or in an area accessible only to qualified or authorized
persons)

Technique(s)

activity assay: suitable

Point isoélectrique

5.4

pl 

5.4

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

2-8°C

InChI

1S/C9H10O3/c1-2-12-9(11)7-3-5-8(10)6-4-7/h3-6,10H,2H2,1H3

Clé InChI

NUVBSKCKDOMJSU-UHFFFAOYSA-N

Informations sur le gène

cow ... CAT(280743)

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Description générale

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

Actions biochimiques/physiologiques

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.

Attention

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

Définition de l'unité

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.

Notes préparatoires

2× crystallized

Inhibiteur

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Consulter la Bibliothèque de documents

Trine Juul et al.
The Journal of biological chemistry, 285(28), 21411-21415 (2010-05-11)
Hydroxyurea (HU) is a well tolerated ribonucleotide reductase inhibitor effective in HIV, sickle cell disease, and blood cancer therapy. Despite a positive initial response, however, most treated cancers eventually progress due to development of HU resistance. Although RNR properties influence
Camilla Ciolli Mattioli et al.
Nucleic acids research, 47(5), 2560-2573 (2018-12-28)
The proper subcellular localization of RNAs and local translational regulation is crucial in highly compartmentalized cells, such as neurons. RNA localization is mediated by specific cis-regulatory elements usually found in mRNA 3'UTRs. Therefore, processes that generate alternative 3'UTRs-alternative splicing and
Koodathingal Prakash et al.
Protein science : a publication of the Protein Society, 11(1), 46-57 (2001-12-14)
Catalases, although synthesized from single genes and built up from only one type of subunit, exist in heterogeneous form with respect to their conformations and association states in biological systems. This heterogeneity is not of genetic origin, but rather reflects
Namrta Purwar et al.
Biochemistry, 50(21), 4491-4503 (2011-04-29)
We present the structures of bovine catalase in its native form and complexed with ammonia and nitric oxide, obtained by X-ray crystallography. Using the NO generator 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, we were able to generate sufficiently high NO concentrations within the catalase crystals
Investigation of the binding mechanism and inhibition of bovine liver catalase by quercetin: Multi-spectroscopic and computational study
Samaneh R, et al.
BioImpacts, 7(3), 147?153-147?153 (2017)

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