Microwave effects on immobilized peroxidase chemiluminescence med./bio.

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.

• protein gels (formed by crosslinking bovine serum albumin and horseradish peroxidase)

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.