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P2088

Sigma-Aldrich

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

CAS Number:
9003-99-0
Enzyme Commission number:
1.11.1.7 (BRENDA, IUBMB)
EC Number:
232-668-6
MDL number:
MFCD00071339
UNSPSC Code:
12352204
NACRES:
NA.54

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

Product No.
Description
Pricing

substrate

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

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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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
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
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
Juliette Azimzadeh et al.
The Plant cell, 20(8), 2146-2159 (2008-09-02)
Plant cells have specific microtubule structures involved in cell division and elongation. The tonneau1 (ton1) mutant of Arabidopsis thaliana displays drastic defects in morphogenesis, positioning of division planes, and cellular organization. These are primarily caused by dysfunction of the cortical
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Horseradish Peroxidase (HRP) Enzymes

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Horseradish Peroxidase (HRP) Enzymes

Discover our peroxidase from horseradish enzymes, products, substrates, and inhibitors for your ELISA, immunoassay, and protein application needs.

Horseradish Peroxidase (HRP) Enzymes

Discover our peroxidase from horseradish enzymes, products, substrates, and inhibitors for your ELISA, immunoassay, and protein application needs.

Horseradish Peroxidase (HRP) Enzymes

Discover our peroxidase from horseradish enzymes, products, substrates, and inhibitors for your ELISA, immunoassay, and protein application needs.

Protocols

Spectrophotometric Determination of Reinheitszahl (RZ) for Peroxidase (EC 1.11.1.7)

Reinheitszahl (RZ) is the ratio of absorbance due to hemin (A403, Soret region) to absorbance due to protein (A275).

Spectrophotometric Determination of Reinheitszahl (RZ) for Peroxidase (EC 1.11.1.7)

Reinheitszahl (RZ) is the ratio of absorbance due to hemin (A403, Soret region) to absorbance due to protein (A275).

Spectrophotometric Determination of Reinheitszahl (RZ) for Peroxidase (EC 1.11.1.7)

Reinheitszahl (RZ) is the ratio of absorbance due to hemin (A403, Soret region) to absorbance due to protein (A275).

Spectrophotometric Determination of Reinheitszahl (RZ) for Peroxidase (EC 1.11.1.7)

Reinheitszahl (RZ) is the ratio of absorbance due to hemin (A403, Soret region) to absorbance due to protein (A275).

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