Microwave radiation effects on the thermally driven oxidase of erythrocytes

Abstract

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 at25, 37,40, 42 or 45°C with an aidow 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°C (74 per cent decrease at 45deg;C). Microwave radiation inhibited the decline in residual CL above 37deg;C. At 45deg;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.

Key Words:

• microwave radiation
• concanavalin A
• chemiluminescence
• haemoglobin
• erythrocytes