Figure 7. Chaperone activity of αBI5C and αBT162C proteins and wild-type αB-crystallin. EDTA-induced aggregation of ADH in the absence or presence of wild-type or mutant proteins was measured at 37 °C. In these experiments, 250 µg of ADH was used with or without crystallins. The chaperone activities of the mutants and wild-type proteins were similar when ADH was used as client protein. This study indicates that the mutation did not alter the structure-function of the protein maintained under reducing condition.