Effect of hyperthermia and lipid peroxidation on the erythrocyte membrane structure.

The hyperthermic exposure (39-49 degrees C) of human erythrocyte membranes augmented their lipid peroxidation stimulated by 0.1 mM FeCl3 + 1.5 mM ascorbate while having no significant influence on the non-stimulated lipid peroxidation. No effect of hyperthermia and lipid peroxidation on the post-exposure fluidity of the erythrocyte membrane lipids was found by the fluorescence anisotropy of hexatriene and trimethylaminophenylhexatriene, and excimerization efficiency of pyrene. Exposure to iron/ascorbate increased the accessibility of membrane protein tryptophan residues to acrylamide as judged by fluorescence quenching. These results suggest a higher sensitivity of membrane protein organization than of membrane lipid fluidity to the effect of the system inducing lipid peroxidation.