Oxidation of biological membranes and its inhibition. Free radical chain oxidation of erythrocyte ghost membranes by oxygen.
The oxidation of human and rat erythrocyte ghost membranes by molecular oxygen has been performed in an aqueous suspension at 37 degrees C. A constant rate of oxygen uptake was observed in the presence of radical initiator. alpha-Tocopherol in the membrane suppressed the oxidation and the induction period was clearly observed. alpha-Tocopherol decreased linearly during the induction period and when it was depleted the induction period was over and a rapid oxidation started. The rate of oxidation was proportional to the square root of the rate of initial radical generation. The kinetic chain length, the ratio of the rate of propagation to that of initiation, was long, ranging from 7 to 100. These results indicate that the erythrocyte ghost membranes are oxidized by a free radical chain mechanism by molecular oxygen. Among the fatty acids of membrane lipids, polyunsaturated fatty acids were oxidized exclusively. Proteins as well as polyunsaturated fatty acids were oxidized and the formation of the high- and low-molecular-weight proteins and the decrease of protein bands were observed on gel electrophoresis.
D000578:Amidines; D000818:Animals; D004910:Erythrocyte Membrane; D005231:Fatty Acids, Unsaturated / Q000097:blood; D005609:Free Radicals; D006801:Humans; D008563:Membrane Lipids / Q000097:blood; D010084:Oxidation-Reduction; D010100:Oxygen; D051381:Rats; D014810:Vitamin E
D000578:Amidines; D005231:Fatty Acids, Unsaturated; D005609:Free Radicals; D008563:Membrane Lipids; D014810:Vitamin E; C046728:2,2'-azobis(2-amidinopropane); D010100:Oxygen