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. Author manuscript; available in PMC: 2014 May 28.
Published in final edited form as: Biochemistry. 2013 May 16;52(21):10.1021/bi301662w. doi: 10.1021/bi301662w

Figure 2.

Figure 2

Effects of αA66-80 peptide on chaperone activity of α-crystallin. The kinetics of aggregation were monitored by measuring the light scattering of the samples at 360 nm for 120 min. α-crystallin was preincubated with peptides separately for 1 h in 37°C before the chaperone activity assay. 1 ADH (150 μg), 2 ADH (150 μg) + α-crystallin (50 μg), 3 ADH (150 μg) + α-crystallin (50 μg) + αA43-56 (5 μg), 4 ADH (150 μg) + α-crystallin (50 μg) + αA43-56 (15 μg), 5 ADH (150 μg) +α-crystallin (50 μg) + αA66-80 (5 μg), 6 ADH (150 μg) + α-crystallin (50 μg)+ αA66-80 (15 μg). InsetT SDS-PAGE analysis: Lanes 1–6 are precipitates of chaperone assay samples 1–6. Samples containing αA66-80 peptide (Lanes 5 & 6) have more α-crystallin, ADH substrate and peptide precipitated than samples containing αA43–56 peptide (Lanes 3 & 4).