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C0887

Sigma-Aldrich

Chloroperoxidase from Caldariomyces fumago

buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)

Sinónimos:

Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase

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1250 UNITS
MXP 15,153.00

MXP 15,153.00

Fecha estimada de envío29 de mayo de 2025

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1250 UNITS
MXP 15,153.00

About This Item

Número de CAS:
9055-20-3
Comisión internacional de enzimas:
1.11.1.10 (BRENDA, IUBMB)
Número MDL:
MFCD00130774
Código UNSPSC:
12352204
NACRES:
NA.54

MXP 15,153.00

Fecha estimada de envío29 de mayo de 2025

origen biológico

fungus (Caldariomyces fumago)

Formulario

buffered aqueous suspension

actividad específica

1,000-2,000 units/mg protein (E1%/280)

mol peso

42 kDa

cociente de absorbancia

RZ ~1.0

temp. de almacenamiento

2-8°C

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Aplicación

A useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures.

Acciones bioquímicas o fisiológicas

Chloroperoxidase (CPO) is a 42,000 Da extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group. CPO is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme. It also catalyzes peroxidase-, catalase- and cytochrome P450-type reactions of dehydrogenation, H2O2 decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs).[1]

Definición de unidad

One unit will catalyze the conversion of 1.0 μmole of monochlorodimedon to dichlorodimedon per min at pH 2.75 at 25 °C in the presence of potassium chloride and H2O2.

Forma física

Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5

Inhibidor

Referencia del producto
Descripción
Precios

A3940

1-Aminobenzotriazole

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

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

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Certificados de análisis (COA)

Lot/Batch Number
0000362985
0000283291
0000362985
0000254664
SLCL9490

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R Vázquez-Duhalt et al.
Phytochemistry, 58(6), 929-933 (2001-10-31)
Chloroperoxidase from Caldariomyces fumago was able to chlorinate 17 of 20 aromatic hydrocarbons assayed in the presence of hydrogen peroxide and chloride ions. Reaction rates varied from 0.6 min(-1) for naphthalene to 758 min(-1) for 9-methylanthracene. Mono-, di- and tri-chlorinated
René Ullrich et al.
Applied and environmental microbiology, 70(8), 4575-4581 (2004-08-06)
Agrocybe aegerita, a bark mulch- and wood-colonizing basidiomycete, was found to produce a peroxidase (AaP) that oxidizes aryl alcohols, such as veratryl and benzyl alcohols, into the corresponding aldehydes and then into benzoic acids. The enzyme also catalyzed the oxidation
Ilona F Persoon et al.
Journal of endodontics, 38(1), 72-74 (2011-12-14)
The aim of this study was to explore the antimicrobial effect of vanadium chloroperoxidase (VCPO) reaction products on Enterococcus faecalis biofilms of 4 different strains. Twenty-four-hour biofilms of E. faecalis strains V583, ER5/1, E2, and OS-16 were incubated in mixtures
Alexander N Morozov et al.
Biophysical journal, 100(4), 1066-1075 (2011-02-16)
Molecular dynamics simulations of an explicitly solvated cis-β-methylstyrene/chloroperoxidase-Compound I complex are performed to determine the cause of the high enantiospecificity of epoxidation. From the simulations, a two-dimensional free energy potential is calculated to distinguish binding potential wells from which reaction
Peter Bernhardt et al.
Journal of the American Chemical Society, 133(12), 4268-4270 (2011-03-10)
Halogenases catalyze reactions that introduce halogen atoms into electron-rich organic molecules. Vanadium-dependent haloperoxidases are generally considered to be promiscuous halogenating enzymes that have thus far been derived exclusively from eukaryotes, where their cellular function is often disputed. We now report
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