25810
Chloroperoxidase from Caldariomyces fumago
aqueous suspension, brown, >10,000 U/mL
Synonym(s):
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
biological source
fungus (Caldariomyces fumago)
Quality Level
form
aqueous suspension
concentration
>10,000 U/mL
color
brown
storage temp.
2-8°C
Looking for similar products? Visit Product Comparison Guide
General description
Chloroperoxidase (CPO) is a major heme-containing, synthetic and versatile enzyme, obtained from Caldariomyces fumago.
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) helps in the catalysis of oxidation reactions with the help of hydrogen peroxide. It displays peroxidase, catalase and cytochrome P450-like functions. CPO also plays a role in catalyzing halogenation reactions.
Unit Definition
1 U corresponds to the amount of enzyme which converts 1 μmol of monochlorodimedone to dichlorodimedone per minute at pH 2.75 and 25 °C in the presence of KCl and H2O2.
Physical form
Supplied as a suspension in 0.1 M sodium phosphate pH 4.0.
Other Notes
Oxidation of aminopyrine; Chloroperoxidase, a peroxidase with potential; Chloroperoxidase-catalyzed asymmetric transformations.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Journal of Industrial Microbiology, 7, 235-235 (1991)
Fast and efficient purification of chloroperoxidase from C. fumago
Process. Biochem., 45(2), 279-283 (2010)
Chemical & pharmaceutical bulletin, 37(12), 3347-3350 (1989-12-01)
Although in the absence of halide ion chloroperoxidase did not catalyze the ethylhydroperoxide (EHP)-supported oxidation of aminopyrine, in the presence of Br- or Cl-, chloroperoxidase did catalyze the oxidation of aminopyrine, generating the aminopyrine cation radical (AP+). The initial rate
The Journal of Organic Chemistry, 57, 7265-7265 (1992)
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
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