Figure 5
From: Investigation of the chaperone function of the small heat shock protein — AgsA
Cooperative effect of AgsA and ΔC11 on aggregation prevention. (A) Lysozyme (10 μM) was denatured by 20 mM DTT with the indicated concentration of AgsA in the presence or absence of 10 μM ΔC11 at 37°C for 30 min. (B) Insulin (70 μM) was denatured by 20 mM DTT with the indicated concentration of ΔC11 in the presence or absence of 10 μM AgsA at 25°C for 40 min. The percentage of turbidity (%) showed the ratio of the turbidity of the DTT-denatured lysozyme or insulin with AgsA and/or ΔC11 to the turbidity of the DTT-denatured lysozyme or insulin alone (for details, see the Materials and Methods section). Error bars show the SD from 3 different experiments.