C0887
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)
Sinônimo(s):
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
Faça loginpara ver os preços organizacionais e de contrato
About This Item
Número CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Produtos recomendados
fonte biológica
fungus (Caldariomyces fumago)
forma
buffered aqueous suspension
atividade específica
1,000-2,000 units/mg protein (E1%/280)
peso molecular
42 kDa
razão de absorbância
RZ ~1.0
temperatura de armazenamento
2-8°C
Procurando produtos similares? Visita Guia de comparação de produtos
Aplicação
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.
Ações bioquímicas/fisiológicas
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).
Definição da unidade
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.
forma física
Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5
inibidor
Nº do produto
Descrição
Preços
Código de classe de armazenamento
12 - Non Combustible Liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificados de análise (COA)
Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.
Já possui este produto?
Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.
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
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
Chaonan Li et al.
Applied biochemistry and biotechnology, 165(7-8), 1691-1707 (2011-09-29)
Chloroperoxidase (CPO) is thought to be the most versatile heme-containing enzyme with enormous applications in organic synthesis, biotransformation, pharmaceutical production, and detoxification of environmental pollutants. Any improvement in the stability of this enzyme will greatly enhance its application in the
Kelath Murali Manoj et al.
PloS one, 5(5), e10601-e10601 (2010-05-26)
Many heme enzymes show remarkable versatility and atypical kinetics. The fungal extracellular enzyme chloroperoxidase (CPO) characterizes a variety of one and two electron redox reactions in the presence of hydroperoxides. A structural counterpart, found in mammalian microsomal cytochrome P450 (CYP)
Rabindra Kumar Behera et al.
Journal of inorganic biochemistry, 104(11), 1185-1194 (2010-08-17)
The site specific mutants of the thermophilic P450 (P450 175A1 or CYP175A1) were designed to introduce residues that could act as acid-base catalysts near the active site to enhance the peroxidases activity. The Leu80 in the distal heme pocket of
Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.
Entre em contato com a assistência técnica