Protein involvement in structural transitions of erythrocyte ghosts. Use of thermal gel analysis to detect protein aggregation

In this study, it is shown that systematic temperature-induced protein aggregation occurs on the erythrocyte membrane by intermolecular disulfide bond formation. Specific protein bands disappear from acrylamide gel profiles over rather narrow temperature regions. The aggregation appears to be the result of irreversible structural transitions of the membrane, which can be seen in a sensitive scanning calorimeter. The aggregation of specific proteins in the narrow temperature region of these transitions persists as the transitions are moved around on the temperature axis by varying solution conditions.