To investigate the effects of extremely low frequency electromagnetic fields on the catalytic activity of the enzyme horseradish peroxidase.
Horseradish peroxidase is a membrane bound enzyme in vivo and by this means to consider as insoluble. The catalytic activity of soluble as well as artificial insoluble peroxidase was investigated in this study in vitro. Immobilization was achieved either by entrapment on a gelatin membrane or by covalent attachment on a nylon membrane.
Exposure | Parameters |
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Exposure 1:
50–400 Hz
Exposure duration:
1, 2, 3 and 4 h
|
Frequency | 50–400 Hz |
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Type | |
Waveform | |
Exposure duration | 1, 2, 3 and 4 h |
Exposure source | |
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Setup | A Plexiglas shelf held the samples parallel to the coils and was positioned in the middle of the structure between the two coils. |
Additional info | Two coils were framed on a Plexiglas structure parallel to each other at distance of 10 cm. The temperature during the experiment was kept at 25°C. |
Measurand | Value | Type | Method | Mass | Remarks |
---|---|---|---|---|---|
magnetic flux density | 1 mT | effective value | measured | - | - |
For soluble peroxidase a positive as well as a negative percentage change of the catalytic activity was found caused by electromagnetic field exposure. A positive maximum was noticed at 130 Hz. Depending on the character of immobilization a maximum positive effect was found at 150 Hz (entrapment) and at 170 Hz (covalent attachment), respectively. No negative interaction could be found for insoluble peroxidase.
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