Figure 5 of Raju, Mol Vis 2011; 17:7-15.


Figure 5. Chaperone activity of αAG98R-crystallin monomers measured with different substrates. The assays were performed as described under methods. Nine μg of the mutant and 10 μg of the wild-type proteins were used in assays. A: Thermal aggregation of ADH in the absence or presence of wild-type or αAG98R-crystallin monomer at 37 °C. In each experiment 75 μg of ADH was used. (Red, ADH; blue, + αAG98R-crystallin; green, + wt αA-crystallin). B: Thermal aggregation of βB2-crystallin in the presence of αAG98R-crystallin monomers. In each experiment 150 μg of βB2-crystallin was used. (Red, βB2; blue, +αAG98R-crystallin; green, + wt αA-crystallin). C: Thermal aggregation of CS in the presence and absence of αAG98R-crystallin monomers. In each experiment 75 μg of CS was used. (Red, CS; blue, +αAG98R-crystallin; green,+ wt αA-crystallin). D: Thermal aggregation of ovotransferrin in presence or absence of αAG98R-crystallin monomers. In each experiment 100 μg of ovotransferrin was used. (Red, ovotransferrin; blue, +αAG98R-crystallin; green, + wt αA-crystallin).