Study type: Medical/biological study (experimental study)

Intensity-dependent effects of microwave electromagnetic fields on acetylcholinesterase activity and protein conformation in frog skeletal muscles med./bio.

Published in: Med Sci Monit 2005; 11 (2): BR50-BR56

Aim of study (acc. to author)

To study the effects of continuous microwaves of different field intensities on acetylcholinesterase activity and protein conformation in muscle fractions from frog skeletal muscles.

Endpoint

Exposure

Exposure Parameters
Exposure 1: 2.45 GHz
Modulation type: CW
Exposure duration: continuous for 30 min
Exposure 2: 2.45 GHz
Modulation type: CW
Exposure duration: continuous for 30 min

Exposure 1

Main characteristics
Frequency 2.45 GHz
Exposure duration continuous for 30 min
Modulation
Modulation type CW
Exposure setup
Exposure source
  • not specified
Sham exposure A sham exposure was conducted.
Additional info the petri dishes maintained at 1.8 and 2°C.
Parameters
Measurand Value Type Method Mass Remarks
SAR 4.92 W/g mean calculated - -
power density 100 W/m² mean measured - -

Exposure 2

Main characteristics
Frequency 2.45 GHz
Exposure duration continuous for 30 min
Modulation
Modulation type CW
Exposure setup
Exposure source
Parameters
Measurand Value Type Method Mass Remarks
power density 200 W/m² mean measured - -
SAR 9.83 W/g mean calculated - -

Reference articles

Exposed system:

Methods Endpoint/measurement parameters/methodology

Investigated system:
Time of investigation:
  • after exposure

Main outcome of study (acc. to author)

Exposure to microwaves results in non-thermal, intensity-dependent, prolonged modification of acetylcholinesterase activity in frog skeletal muscles traced up to 48 hours after irradiation. A significant decrease in enzyme activity on the day of exposure was revealed. 48 hours later the decrease in enzyme activity in samples exposed to both high- and low-intensity microwaves was less than that in sham-exposed samples.
Infrared spectroscopy data argue for microwave-induced conformational changes in the secondary structure of muscle proteins: increased content of beta-structures, random coils, and amorphous structures, which were more expressed at irradiation with low field intensity.

Study character:

Study funded by

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