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C3155

Sigma-Aldrich

Catalase from bovine liver

aqueous solution, ≥30,000 units/mg protein

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Synonym(s):
H2O2:H2O2 oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.32

biological source

bovine liver

Quality Level

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.

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)

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This Item
C100C9322C1345
vibrant-m

C3155

Catalase from bovine liver

vibrant-m

C100

Catalase from bovine liver

vibrant-m

C9322

Catalase from bovine liver

vibrant-m

C1345

Catalase from bovine liver

biological source

bovine liver

biological source

-

biological source

bovine liver

biological source

bovine liver

Quality Level

200

Quality Level

200

Quality Level

400

Quality Level

200

form

aqueous solution

form

aqueous suspension

form

lyophilized powder

form

powder

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

Gene Information

cow ... CAT(280743)

Gene Information

cow ... CAT(280743)

Gene Information

cow ... CAT(280743)

Gene Information

cow ... CAT(280743)

General description

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, catalses 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.

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 catalyzes the degradation of hydrogen peroxide into 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.

Components

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.

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.

Inhibitor

Product No.
Description
Pricing

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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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
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
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)
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
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

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