C0887
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)
Synonym(s):
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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1250 UNITS
CZK 18,000.00
CZK 18,000.00
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
1,000-2,000 units/mg protein (E1%/280)
Biological source:
fungus (Caldariomyces fumago)
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biological 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
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1 of 4
This Item | |||
|---|---|---|---|
| biological source fungus (Caldariomyces fumago) | biological source - | biological source fungus (Caldariomyces fumago) | biological source Aspergillus niger |
| specific activity 1,000-2,000 units/mg protein (E1%/280) | specific activity - | specific activity - | specific activity ≥4,000 units/mg protein |
| 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 |
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.
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flash_point_f
Not applicable
flash_point_c
Not applicable
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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
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
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
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C0887-1.25KU | 04061832728971 |
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