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C0887

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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Tamaño de envaseSKUDisponibilidadPrecio
1250 units

Disponible para enviar HOYdesdeMILWAUKEE

$816.00

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Número CAS:
9055-20-3
UNSPSC Code:
12352204
NACRES:
NA.54
Número CE:
1.11.1.10 (BRENDA, IUBMB)
MDL number:
MFCD00130774
Specific activity:
1,000-2,000 units/mg protein (E1%/280)
Biological source:
fungus (Caldariomyces fumago)

$816.00

Disponible para enviar HOYDetalles

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biological source

fungus (Caldariomyces fumago)

Quality Level

200

form

buffered aqueous suspension

specific activity

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

mol wt

42 kDa

absorbance ratio

RZ ~1.0

storage temp.

2-8°C

Application

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.

Biochem/physiol Actions

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]

Physical form

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

Other Notes

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.

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Este artículo
C027825810C3515
Chloroperoxidase from Caldariomyces fumago buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)

Sigma-Aldrich

C0887

Chloroperoxidase from Caldariomyces fumago

Chloroperoxidase from Caldariomyces fumago buffered aqueous suspension, ≥3,000 units/mL

Sigma-Aldrich

C0278

Chloroperoxidase from Caldariomyces fumago

Chloroperoxidase from Caldariomyces fumago aqueous suspension, brown, >10,000 U/mL

Sigma-Aldrich

25810

Chloroperoxidase from Caldariomyces fumago

Catalase from Aspergillus niger ammonium sulfate suspension, ≥4,000 units/mg protein

Sigma-Aldrich

C3515

Catalase from Aspergillus niger

specific activity

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

specific activity

-

specific activity

-

specific activity

≥4,000 units/mg protein

biological source

fungus (Caldariomyces fumago)

biological source

-

biological source

fungus (Caldariomyces fumago)

biological source

Aspergillus niger

form

buffered aqueous suspension

form

buffered aqueous suspension

form

aqueous suspension

form

ammonium sulfate suspension

mol wt

42 kDa

mol wt

42 kDa

mol wt

-

mol wt

tetramer ~250 kDa

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

100

Quality Level

200

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Certificados de análisis (COA)

Lot/Batch Number
0000362985
0000283291
0000283291
0000362985
0000254664

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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
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
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
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Número de artículo de comercio global

SKUGTIN
C0887-1.25KU04061832728971

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