C0278
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, ≥3,000 units/mL
Synonym(s):
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Product Name
Chloroperoxidase from Caldariomyces fumago, buffered aqueous suspension, ≥3,000 units/mL
form
buffered aqueous suspension
mol wt
42 kDa
concentration
≥3,000 units/mL
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Looking for similar products? Visit Product Comparison Guide
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.
Chloroperoxidase from Caldariomyces fumagois is useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures. It has been used to study biocatalytic oxidation in polymersome nanoreactors .
It has been used to study biocatalytic oxidation in polymersome nanoreactors.
Biochem/physiol Actions
Chloroperoxidase (CPO) is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase, catalase and cytochrome P450-type reactions of dehydrogenation, hydrogenperoxide (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). PAHs are considered to be a potential health risk because of their possible carcinogenic and mutagenic activities and are widely dispersed in the environment.
General description
Chloroperoxidase is a heme containing glycoprotein that is secreted from fungus. Chloroperoxidase (CPO) is a extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group.
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.
Physical form
Crude suspension in 0.1 M sodium phosphate, pH ~4.5
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
常规特殊物品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
C M Hosten et al.
The Journal of biological chemistry, 269(19), 13966-13978 (1994-05-13)
Near-ultraviolet resonance Raman spectra of chloroperoxidase derivatives and high valent intermediates show frequencies that can be systematically assigned. In accord with previous observations of low v4 frequencies for the ferric enzyme, and quite low v4 frequencies for the ferrous enzyme
Brett L Allen et al.
ACS nano, 5(6), 5263-5272 (2011-05-21)
Poly(propylene sulfide) nanoparticles (<150 nm) have been synthesized by an anionic, ring-opening emulsion polymerization. Upon exposure to parts per million (ppm) levels of oxidizing agent (NaOCl), hydrophobic polysulfide particles are oxidized to hydrophilic polysulfoxides and polysulfones. Utilizing this mechanism, the
Clarisse B S Roepcke et al.
Journal of agricultural and food chemistry, 58(15), 8748-8756 (2010-07-10)
Acetylcholinesterase (AChE) is responsible for the hydrolysis of acetylcholine in the nervous system. It is inhibited by organophosphate and carbamate pesticides. However, this enzyme is only slightly inhibited by organophosphorothionates, which makes the detection of these pesticides analytically very difficult.
Markus Buchhaupt et al.
Biotechnology letters, 33(11), 2225-2231 (2011-07-08)
The filamentous fungus Caldariomyces fumago secretes a chloroperoxidase (CPO). To increase its production, we integrated a CPO-expression cassette into the non-transcribed spacer regions of the rDNA in C. fumago. One strain was obtained that had twice the CPO activity when
Xinting Yuan et al.
Journal of inorganic biochemistry, 104(11), 1156-1163 (2010-08-03)
Oxidation of the heme-thiolate enzyme chloroperoxidase (CPO) from Caldariomyces fumago with peroxynitrite (PN) gave the Compound II intermediate, which was photo-oxidized with 365 nm light to give a reactive oxidizing species. Cryo-solvents at pH ≈ 6 were employed, and reactions
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service