Microwave radiation effects on the thermally driven oxidase of erythrocytes.
Sheep red blood cells (SRBCs) were labelled with a concanavalin A-luminol-bovine serum albumin conjugate specific for the transmembrane anion transport protein (Band 3) and exposed to 2450 MHz continuous wave microwave radiation at an average specific absorption rate of 91 W/kg for 10 min. The temperature was held constant at 25, 37, 40, 42 or 45 degrees C with an airflow heat exchange system. Following exposure to microwave or air heating, the decrease in residual base-activated chemiluminescence (CL) of the SRBCs was measured as an indication of infield oxidase activity. Air heating resulted in a significant decrease in residual CL at temperatures above 37 degrees C (74 per cent decrease at 45 degrees C). Microwave radiation inhibited the decline in residual CL above 37 degrees C. At 45 degrees C the inhibition was 40 per cent. The results suggest microwave radiation either reversibly altered the thermodynamics of oxygen binding to haemoglobin or failed to energize a significant portion of the haemoglobin molecules in each sample to the thermal threshold of haemoglobin autoxidation.
D000818:Animals; D003208:Concanavalin A / Q000378:metabolism; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology / Q000528:radiation effects*; D006461:Hemolysis / Q000528:radiation effects; D006358:Hot Temperature; D006861:Hydrogen Peroxide / Q000378:metabolism; D008163:Luminescent Measurements; D008165:Luminol / Q000378:metabolism; D008872:Microwaves; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012756:Sheep
D003208:Concanavalin A; D012710:Serum Albumin, Bovine; D008165:Luminol; D006861:Hydrogen Peroxide; D010088:Oxidoreductases