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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 3.

Figure 3

αA66-80-induced aggregation of α-crystallin. (A) α-crystallin (5 μM) incubated with αA66-80 (25 μM) in 1 ml of 50 mM phosphate buffer monitored at 360 nm at different durations of incubation (data presented as mean ± SD of 3 independent measurements). (B) The concentration of soluble proteins at different time points during incubation (data represented as mean ± SD of 3 independent measurements). (C) SDS-PAGE analysis: α-crystallin (10 μM) was incubated with different concentrations of αA66-80 (1.25 μM- 20 μM) in 1ml of 50 mM phosphate buffer (pH 7.2) at 37°C for 24 h. After incubation, samples were centrifuged at 8000 rpm for 15 min and pellets were dissolved in SDS-PAGE sample buffer and run in 4–20% gel. α: αA66-80 ratio - Lane 1 - 1: 0 μM, Lane 2 - 1: 0.125 μM, Lane 3 - 1: 0.25 μM, Lane 4 - 1: 0.5 μM, Lane 5 - 1: 1 μM, Lane 6 - 1: 1.5 μM, Lane 7 - 1: 2 μM.