Modification of membrane protein organization during in vitro aging of human erythrocytes.
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. SDS-polyacrylamide gel electrophoresis after dithiothreitol dissociation indicates that the aggregates are made of peptide fragments with a molecular weight ranging from 20 to approximately 110 kdalton; none of these fragments correspond to an intact protein component of the membrane. Their formation results from oxidation and proteolysis of membrane, and perhaps cytoplasmic proteins.
D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004229:Dithiothreitol / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004905:Erythrocyte Aging; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism*
D000596:Amino Acids; D008565:Membrane Proteins; D004229:Dithiothreitol