PROTEIN AGGREGATION IN INTACT AND DISRUPTED PEROXIDIZING ERYTHROCYTE MEMBRANES

Abstract

The effects of molecular organization on the interaction of peroxidizing lipids with proteins were studied by using human red cell membranes. Intact and chloroform-disrupted membranes were oxidized. Disruption of membranes was achieved by treatment with chloroform and subsequent elimination of the solvent. Lipid oxidation rates and SDS-electrophoretic protein patterns in the two types of membranes were compared. Specific 3H-DIDS label of band 3 allowed the study of the role of intrinsic proteins in the aggregation process. Lipid oxidation rate is not greatly affected by chloroform disruption although disrupted membranes show a higher rate of protein aggregation. α-Tocopherol decreases lipid oxidation and protein aggregation rates. Band 3 protein dimers (188,000 M.W.) appear earlier than the higher molecular weight protein aggregates (400,000 M.W.). The results suggest that native membrane organization prevents protein damage upon lipid peroxidation.