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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.
| Abbreviations | ||
| LPO | = | lactoperoxidase |
| MPO | = | myeloperoxidase |
| EPO | = | eosinophil peroxidase |
| TPO | = | thyroid peroxidase |
| Nox4 | = | NADPH oxidase 4 |
| ROS | = | reactive oxygen species |
| HPLC | = | high performance liquid chromatography |
| MS | = | mass spectrometry |
| DT | = | dityrosine. |
| Abbreviations | ||
| LPO | = | lactoperoxidase |
| MPO | = | myeloperoxidase |
| EPO | = | eosinophil peroxidase |
| TPO | = | thyroid peroxidase |
| Nox4 | = | NADPH oxidase 4 |
| ROS | = | reactive oxygen species |
| HPLC | = | high performance liquid chromatography |
| MS | = | mass spectrometry |
| DT | = | dityrosine. |