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. Author manuscript; available in PMC: 2014 May 1.
Published in final edited form as: Exp Eye Res. 2013 Mar 4;110:10–17. doi: 10.1016/j.exer.2013.02.016

Fig. 1. αB-crystallin R120G has decreased and αB-crystallin M68A increased chaperone activity levels relative to wt αB-crystallin.

Fig. 1

Chaperone activities of purified recombinant wt αB-crystallin, αB-crystallin R120G, and αB-crystallin M68A using lysozyme as a target substrate. Lysozyme was incubated in the presence or absence of wt αB-crystallin or αB-crystallin mutants R120G and M68A in the presence of absence of 20 mM DTT and protein aggregation monitored by measuring absorbance (turbidity) at 360nm. Graph shows mean values of n=3 ± SD. p values were calculated using two sample Student t-test assuming equal variance. Significant differences between wt and mutants are shown wt - R120G, p<0.05, wt - M68A, p<0.001.