To determine if radiofrequency radiation (RFR) influences local or overall immobilized peroxidase activity (peroxidase was covalently crosslinked with another protein to form a gel) at a constant temperature through following potential mechanisms: 1) the electric fields may influence the electron flow and subsequent reduction-oxidation activity of the gel, 2) RFR influence on orientation and alignment of protein molecules during gel formation resulting in changes in local enzymatic activity, 3) the diffusion rate of mobile substrate through the gel may be influenced by nonuniformity of energy deposition (SAR) in the gel.
|Exposure duration||30 min|
During exposure, a significant reversible increase occured in overall mean peroxidase activity of gels activated with 0.88 M H2O2 but not in those gels 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 change in the distribution of local activities when compared to unexposed gels. These results are apparently due to alterations in the rate of diffusion of H2O2 in the gel.