Description

• 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. [1] It has also been used to help develop a colorimetric method for microRNA (miRNA) detection by creating a horseradish peroxidase-mimicking DNAzyme. [2]
• Biochem/physiol Actions: Horseradish peroxidase has been shown to catalyze the polymerization of various substances including acetaminophen and cardanol. [3][4]
• 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.