C0278
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, ≥3,000 units/mL
Synonyme(s) :
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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6250 UNITS
556.00 CHF
12500 UNITS
1 030.00 CHF
556.00 CHF
Date d'expédition estimée le08 avril 2025
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6250 UNITS
556.00 CHF
12500 UNITS
1 030.00 CHF
About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
556.00 CHF
Date d'expédition estimée le08 avril 2025
Produits recommandés
Forme
buffered aqueous suspension
Niveau de qualité
Poids mol.
42 kDa
Concentration
≥3,000 units/mL
Conditions d'expédition
wet ice
Température de stockage
2-8°C
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Description générale
Chloroperoxidase is a heme containing glycoprotein that is secreted from fungus. Chloroperoxidase (CPO) is a extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group.[1]
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.
Chloroperoxidase from Caldariomyces fumagois is useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures. It has been used to study biocatalytic oxidation in polymersome nanoreactors [2].
It has been used to study biocatalytic oxidation in polymersome nanoreactors.[2]
Actions biochimiques/physiologiques
Chloroperoxidase (CPO) is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase, catalase and cytochrome P450-type reactions of dehydrogenation, hydrogenperoxide (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). PAHs are considered to be a potential health risk because of their possible carcinogenic and mutagenic activities and are widely dispersed in the environment.[3]
Définition de l'unité
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.
Forme physique
Crude suspension in 0.1 M sodium phosphate, pH ~4.5
Inhibiteur
Réf. du produit
Description
Tarif
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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C M Hosten et al.
The Journal of biological chemistry, 269(19), 13966-13978 (1994-05-13)
Near-ultraviolet resonance Raman spectra of chloroperoxidase derivatives and high valent intermediates show frequencies that can be systematically assigned. In accord with previous observations of low v4 frequencies for the ferric enzyme, and quite low v4 frequencies for the ferrous enzyme
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
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
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
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