Abstract
The aim of this work was to study the dityrosine-forming activity of lactoperoxidase (LPO) and its potential application for measuring hydrogen peroxide (H2O2). It was observed that LPO was able to form dityrosine at low H2O2 concentrations. Since dityrosine concentration could be measured in a simple fluorimetric reaction, this activity of the enzyme was utilized for the measurement of H2O2 production in different systems. These experiments successfully measured the activity of NADPH oxidase 4 (Nox4) by this method. It was concluded that LPO-mediated dityrosine formation offers a simple way for H2O2 measurement.
Publication types
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Evaluation Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cattle
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Cell Line
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Chromatography, High Pressure Liquid
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Fluorometry / methods
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Glucose / metabolism
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Glucose Oxidase / metabolism
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Humans
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Hydrogen Peroxide / analysis*
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Hydrogen Peroxide / metabolism
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In Vitro Techniques
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Lactoperoxidase / isolation & purification
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Lactoperoxidase / metabolism*
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Mass Spectrometry
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Milk / enzymology
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NADPH Oxidase 4
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NADPH Oxidases / genetics
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NADPH Oxidases / metabolism
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Reactive Oxygen Species / metabolism
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Transfection
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Tyrosine / analogs & derivatives*
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Tyrosine / biosynthesis
Substances
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Reactive Oxygen Species
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Recombinant Proteins
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Tyrosine
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Hydrogen Peroxide
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dityrosine
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Glucose Oxidase
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Lactoperoxidase
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NADPH Oxidase 4
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NADPH Oxidases
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NOX4 protein, human
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Glucose