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Figure 4 | BMC Biochemistry

Figure 4

From: Investigation of the chaperone function of the small heat shock protein — AgsA

Figure 4

Interaction denatured insulin with AgsA and/or ΔC11. (A) Insulin (10 μM) was denatured in the presence of AgsA (50 μM) at 25°C or 50°C, and then analysed using size exclusion chromatography at 25°C. (B) Insulin (10 μM) was denatured in the presence of ΔC11 (50 μM) or AgsA (25 μM) and ΔC11 (25 μM) at 25°C, and then analysed using size exclusion chromatography. An aliquot of each fraction (200 μl) was excited at 490 nm and the fluorescence intensity was determined at 525 nm. The retention volume of the protein molecular weight standards is shown above the panel. Broken black line, insulin was denatured with AgsA at 25°C; red solid line, insulin was denatured with AgsA at 50°C; yellow solid line, insulin was denatured with ΔC11 at 25°C and green solid line, insulin was denatured with AgsA and ΔC11 at 25°C.

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