Organizational differences in the membrane proteins of normal and irreversibly sickled erythrocytes.
Using two-dimensional gels, no unique membrane proteins were detected in irreversibly sickled cells. Membranes from irreversibly sickled cells were shown to cross-link much more readily with dithiobis(succinimidyl propionate) than normal erythrocyte membranes. Increased binding of band 4.5 protein and increased intra-chain disulfides were also demonstrated. These changes may correlate to enhanced cellular rigidity.
D000755:Anemia, Sickle Cell / Q000097:blood*; D055598:Chemical Phenomena; D002621:Chemistry; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000032:analysis* / Q000648:ultrastructure; D004912:Erythrocytes / Q000032:analysis*; D006801:Humans; D008565:Membrane Proteins / Q000097:blood*
D003432:Cross-Linking Reagents; D008565:Membrane Proteins