C0887
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)
Synonim(y):
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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About This Item
Numer CAS:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.54
Polecane produkty
pochodzenie biologiczne
fungus (Caldariomyces fumago)
Postać
buffered aqueous suspension
aktywność właściwa
1,000-2,000 units/mg protein (E1%/280)
masa cząsteczkowa
42 kDa
stosunek absorbancji
RZ ~1.0
temp. przechowywania
2-8°C
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Zastosowanie
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.
Działania biochem./fizjol.
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).
Definicja jednostki
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.
Postać fizyczna
Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5
This page may contain text that has been machine translated.
inhibitor
Numer produktu
Opis
Cennik
Kod klasy składowania
12 - Non Combustible Liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Środki ochrony indywidualnej
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certyfikaty analizy (CoA)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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
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
Rosario Médici et al.
Biotechnology letters, 33(10), 1999-2003 (2011-06-11)
The synthesis of halogenated nucleosides and nucleobases is of interest due to their chemical and pharmacological applications. Herein, the enzymatic halogenation of nucleobases and analogues catalysed by microorganisms and by chloroperoxidase from Caldariomyces fumago has been studied. This latter enzyme
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