| Abstract: | Protein gels formed by crosslinking bovine serum albumin and horseradish peroxidase with glutaraldehyde were used to measure effects on peroxidase activity of 400-MHz (CW) radiofrequency radiation (RFR) at an average specific absorption rate (SAR) of 1.45 W/kg. The enzyme activity was measured by luminol chemiluminescence recorded on photographic film after hydrogen peroxide activation. Activity was measured during RFR exposure of gels or after exposure of gels polymerized in the RFR field. During exposure, a significant (P less than .05) reversible increase occurred in overall mean peroxidase activity of gels activated with 0.88 M H2O2 but not in those activated with 8.8 M H2O2. Gels containing solubilized luminol and formed in the field showed no overall mean increase in peroxidase activity, but did display a highly significant (P less than .001) alteration in the distribution of local activities when compared to unexposed gels. These results are apparently due to changes in the rate of diffusion (concentration equilibration) of hydrogen peroxide in the gel. |
