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Erythrocytes are enucleated cells with plasma membrane envelope. Erythrocytes owing to its oxygen transport function are susceptible to continuous oxidative stress. The impact of this oxidative stress could affect the integrity of the erythrocyte membrane and thereby its constituents. Henceforth, the present study aimed to analyse the erythrocyte membrane protein changes in response to water-soluble pro-oxidant, hydrogen peroxide (H2O2) and lipophilic pro-oxidant, tertiary butyl hydroperoxide (t-BuOOH). The erythrocyte lysate after subjected to H2O2 and t-BuOOH additions at various concentrations in the range 1 mM to 6 mM were subjected to electrophoresis (SDS-PAGE). We observed that the band intensity of most of the erythrocyte membrane proteins such as ankyrin, catalase, actin, glutathione peroxidase and peroxiredoxin appeared to fade upon increasing concentration of both pro-oxidants. This implicated that upon increasing oxidative stress, erythrocyte membrane proteins could be modified by oxidation and loses its very function of maintaining the integrity of the cell.