Merck
All Photos(1)

C30

Sigma-Aldrich

Catalase from bovine liver

aqueous suspension, 10,000-40,000 units/mg protein

Synonym(s):
H2O2:H2O2 oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:
eCl@ss:
32160410
NACRES:
NA.54

biological source

bovine liver

Quality Level

form

aqueous suspension

specific activity

10,000-40,000 units/mg protein

mol wt

tetramer ~250 kDa

concentration

20-50 mg/mL

isoelectric point

5.4

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

Gene Information

cow ... CAT(280743)

Looking for similar products? Visit Product Comparison Guide

General description

Catalase from bovine liver contains 506 residues.[1] 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.[2]

Application

Catalase from bovine liver has been used for measuring the hydrogen peroxide conetent in cancer tissue homogenates.[3] 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.[4]
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.[5][6]
  • GC-MS analyses.[7]
  • Deionization.[8]
  • GC-FID analysis.5
  • Functional analysis of blood vessel.[9]
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

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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

Product Information Sheet

More Documents

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service