Figure 2 of Rao, Mol Vis 2008; 14:666-674.


Figure 2. Chaperone-like activity of αB-crystallin-βA3/A1102–117 peptide complex against denaturing βL-crystallin. βL-crystallin (100 μg) was incubated at 55 °C in presence of 5 μg and 10 μg of αB-crystallin or αB-crystallin-βA3/A1102–117 peptide complex for 60 min and the light scattering was measured as described under methods. The results show that prior interaction of αB-crystallin with βA3/A1102-117 peptide diminished its chaperone-like activity against denaturing βL-crystallin. A, βL-crystallin; B, βL-crystallin + 5 μg αB-crystallin; C, βL-crystallin + 10 μg αB-crystallin; D, βL-crystallin + 5 μg αB-crystallin-βA3/A1102–117 peptide complex; E, βL-crystallin + 10 μg αB-crystallin-βA3/A1102–117 peptide complex; F, αB-crystallin or αB-crystallin-βA3/A1102–117 peptide complex alone. Insert: Relative light scattering by βL-crystallin in presence of αB-crystallin or αB-crystallin-βA3/A1102–117 peptide complex. Scattering by βL-crystallin alone at 60 min is considered to be 100%.