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
Autenticati per visualizzare i prezzi organizzativi e contrattuali.
Scegli un formato
Cambia visualizzazione
| Taglio della confezione | SKU | Disponibilità | Prezzo |
|---|---|---|---|
| 1250 units | Per conoscere la disponibilità, visualizza il carrello | CHF 662.00 |
Informazioni su questo articolo
Numero CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
1,000-2,000 units/mg protein (E1%/280)
Biological source:
fungus (Caldariomyces fumago)
CHF 662.00
Per conoscere la disponibilità, visualizza il carrello
Servizio Tecnico
Hai bisogno di aiuto? Il nostro team di scienziati qualificati è a tua disposizione.
Permettici di aiutartibiological source
fungus (Caldariomyces fumago)
Quality Level
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
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]
Physical form
Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5
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.
1 of 1
Questo articolo | |||
|---|---|---|---|
| specific activity 1,000-2,000 units/mg protein (E1%/280) | specific activity - | specific activity - | specific activity ≥4,000 units/mg protein |
| biological source fungus (Caldariomyces fumago) | biological source - | biological source fungus (Caldariomyces fumago) | biological source Aspergillus niger |
| 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 |
Classe di stoccaggio
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)
Scegli una delle versioni più recenti:
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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
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
Numero articolo commerciale globale
| SKU | GTIN |
|---|---|
| C0887-1.25KU | 04061832728971 |