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.