1. 1. In in vitro aged human erythrocytes, the presence of protein clusters can be found on the membrane; these clusters are made up of peptides held together by disulfide bridges, since they can be nearly completely dissociated by dithiothreitol treatment. 2. 2. SDS-polyacrylamide gel electrophoresis after dithiothreitol dissociation indicates that the aggregates are made of peptide fragments with a molecular weight ranging from 20 to ~ 110 kdalton; none of these fragments correspond to an intact protein component of the membrane. 3. 3. Their formation results from oxidation and proteolysis of membrane, and perhaps cytoplasmic proteins.
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