Figure 2
From: Investigation of the chaperone function of the small heat shock protein — AgsA
Chaperone activity of the truncated AgsA in the Δ rpoH mutant. The cells were grown in LB medium supplement with 1 mM IPTG at 30°C for 3 h and further cultured at 42°C for 1 h. Total proteins and aggregated proteins were isolated as described in the Materials and Methods. Equal amounts of total proteins (10 μg) were analyzed by 15% SDS-PAGE. The stained gels were scanned and the level of AgsA and its truncated mutants were quantified. Line graph and right ordinate show the relative amount of truncated AgsA with the amount of AgsA set to 1. Bar graph and left ordinate show the percentage of aggregated protein calculated by the ratio of the aggregated protein and the total protein. Error bars show the SD from 3 different experiments.