Figure 2. The chaperone ability of wild-type and C-terminal mutants of αB-crystallin to prevent amorphous aggregation.

A, Heat-induced precipitation of β_L-crystallin at 60°C and C, DTT-induced precipitation of insulin B-chain at 37°C, in the absence or presence of wild-type and mutant αB-crystallins at a 1.0:0.2 molar ratio of β_L-crystallin: αB-crystallin and a 1.0:0.14 molar ratio of insulin: αB-crystallin. The change in light scattering at 340 nm for each sample is shown. Each assay was repeated four times and the data shown are representative. B and D show the percentage protection for each protein in the β_L-crystallin and insulin B-chain aggregation assays respectively. The data in B and D represent the mean±standard error of the mean (SEM) of the 4 different experiments, * denotes a significant (p<0.05) difference in the mean compared to wild-type αB-crystallin.