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C0887

Chloroperoxidase from Caldariomyces fumago

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

Synonym(s):

Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase

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1250 UNITS

$816.00

$816.00

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About This Item

CAS Number:
9055-20-3
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
1.11.1.10 (BRENDA, IUBMB)
MDL number:
MFCD00130774

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Product Name

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

biological source

fungus (Caldariomyces fumago)

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

Quality Level

200

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This Item
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

biological source

fungus (Caldariomyces fumago)

biological source

-

biological source

fungus (Caldariomyces fumago)

biological source

Aspergillus niger

specific activity

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

specific activity

-

specific activity

-

specific activity

≥4,000 units/mg protein

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

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]

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.

Physical form

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

related product

Product No.
Description
Pricing

A3940

1-Aminobenzotriazole

Storage Class

12 - Non Combustible Liquids

wgk

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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Certificates of Analysis (COA)

Lot/Batch Number
0000362985
0000283291
0000283291
0000362985
0000254664

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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
Daniel Andrew et al.
Biochemical and biophysical research communications, 415(4), 646-649 (2011-11-15)
Azide is a well-known inhibitor of heme-enzymes. Herein, we report the counter-intuitive observation that at some concentration regimes, incorporation of azide in the reaction medium enhances chloroperoxidase (CPO, a heme-enzyme) mediated one-electron abstractions from several substrates. A diffusible azidyl radical
Marcela Ayala et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 16(1), 63-68 (2010-09-14)
Heme peroxidases are subject to a mechanism-based oxidative inactivation. During the catalytic cycle, the heme group is activated to form highly oxidizing species, which may extract electrons from the protein itself. In this work, we analyze changes in residues prone
Sudeep Kumar Gade et al.
Biochemical and biophysical research communications, 419(2), 211-214 (2012-02-22)
We report that incorporation of very low concentrations of redox protein cytochrome c and redox active small molecule vitamin C impacted the outcome of one-electron oxidations mediated by structurally distinct plant/fungal heme peroxidases. Evidence suggests that cytochrome c and vitamin
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