P2088
Peroxidase from horseradish
Highly stabilized, essentially salt-free, lyophilized powder, 200-300 units/mg solid (using pyrogallol)
Synonym(s):
Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase
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About This Item
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biological source
horseradish
form
essentially salt-free, lyophilized powder
specific activity
200-300 units/mg solid (using pyrogallol)
mol wt
~44 kDa
absorbance ratio
RZ 2.6-3.4
storage temp.
2-8°C
InChI
1S/H2O3/c1-3-2/h1-2H
InChI key
JSPLKZUTYZBBKA-UHFFFAOYSA-N
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General description
Horseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.
Application
Peroxidase from horseradish has been used in a study with dehydrogenative polymers (DHP) to investigate the monolignol coupling mechanism. It has also been used to help develop a colorimetric method for microRNA (miRNA) detection by creating a horseradish peroxidase-mimicking DNAzyme.
Biochem/physiol Actions
Horseradish peroxidase has been shown to catalyze the polymerization of various substances including acetaminophen and cardanol.
Caution
Maintains activity at low pH and higher temperature.
Unit Definition
One pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.
Preparation Note
Stabilized by chemical protection of the primary amines.
Analysis Note
The RZ (Reinheitszahl) is the absorbance ratio A403/A275 determined at 0.5-1.0 mg/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.
Other Notes
View more information on peroxidase at www.sigma-aldrich.com/enzymeexplorer.
inhibitor
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Description
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substrate
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Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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D W Potter et al.
Molecular pharmacology, 29(2), 155-162 (1986-02-01)
Horseradish peroxidase catalyzed the polymerization of acetaminophen. Addition of reduced glutathione (GSH) to reaction mixtures resulted in decreased polymerization and formation of minor amounts of GSH-acetaminophen conjugates. The conjugates were identified as 3-(glutathion-S-yl)acetaminophen and 3-(glutathion-S-yl)diacetaminophen. Horseradish peroxidase also catalyzed polymerization
Yanqin Wen et al.
Analytical chemistry, 84(18), 7664-7669 (2012-08-30)
We present a highly sensitive colorimetric method for microRNA (miRNA) detection. This method is based on a rolling-circle amplification (RCA) DNA machine, which integrates RCA, nicking enzyme signal amplification and DNAzyme signal amplification. The DNA machine is triggered by the
Keehoon Won et al.
Biomacromolecules, 5(1), 1-4 (2004-01-13)
Horseradish peroxidase-catalyzed polymerization of cardanol in aqueous organic solvent was investigated in the presence of a redox mediator. Cardanol is a phenol derivative from a renewable resource mainly having a C15 unsaturated hydrocarbon chain with mostly 1-3 double bonds at
Sun-Joo Moon et al.
Phytochemistry, 82, 15-21 (2012-08-14)
In this study, dehydrogenative polymers (DHP) were synthesized in vitro through dehydrogenative polymerization using different ratios of coniferyl alcohol (CA) and sinapyl alcohol (SA) (10:0, 8:2, 6:4, 2:8, 0:10), in order to investigate the monolignol coupling mechanism in the presence
Jane M Natividad et al.
PloS one, 4(7), e6472-e6472 (2009-08-04)
Excessive uptake of commensal bacterial antigens through a permeable intestinal barrier may influence host responses to specific antigen in a genetically predisposed host. The aim of this study was to investigate whether intestinal barrier dysfunction induced by indomethacin treatment affects
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