C0887
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)
Sinonimo/i:
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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1250 UNITS
659,00 €
659,00 €
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Cambia visualizzazione
1250 UNITS
659,00 €
About This Item
Numero CAS:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54
659,00 €
Per informazioni sulla disponibilità, contatta il Servizio Clienti.
Prodotti consigliati
Origine biologica
fungus (Caldariomyces fumago)
Stato
buffered aqueous suspension
Attività specifica
1,000-2,000 units/mg protein (E1%/280)
PM
42 kDa
Rapporto di assorbanza
RZ ~1.0
Temperatura di conservazione
2-8°C
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Applicazioni
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.
Azioni biochim/fisiol
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]
Definizione di unità
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.
Stato fisico
Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5
Inibitore
N° Catalogo
Descrizione
Determinazione del prezzo
Codice della classe di stoccaggio
12 - Non Combustible Liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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
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
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
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
Adam C Chamberlin et al.
The journal of physical chemistry. B, 115(13), 3642-3647 (2011-03-18)
OLYP/TZP calculations on two symmetrized model complexes [Fe(TPP)(py)(2)](2+) and [Fe(TPP)(PhNC)(2)](2+) (TPP = meso-tetraphenylporphyrin, py = pyridine, PhNC = phenylisocyanide) reveal dense manifolds of low-energy electronic states. For the latter complex, broken-symmetry calculations successfully reproduce the unique S = 0 ground
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