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. 2009 May 6;284(26):17641–17647. doi: 10.1074/jbc.M109.007070

FIGURE 2.

FIGURE 2.

Chaperone activity of P3H1·CRTAP·CypB complex using citrate synthase as a substrate. The inhibition of the thermal aggregation of citrate synthase by the P3H1·CRTAP·CypB complex was monitored at 500 nm. A 30 μm citrate synthase solution was diluted 200-fold into prewarmed 40 mm Hepes buffer, pH 7.5, at 43 °C. A, in the absence (black) and presence of 0.001 (red), 0.0025 (green), 0.005 (blue), and 0.01 μm (orange) P3H1·CRTAP·CypB complex. B, in the absence (black) and presence of 0.01 μm complex (red), 0.15 μm protein-disulfide isomerase (blue), and 0.15 μm bovine serum albumin (green). C, in the absence (black) and presence of 1 μm cyclosporine A (red) with 0.01 μm CypB (blue), with 0.005 μm P3H1·CRTAP·CypB complex (green), and with 0.005 μm P3H1·CRTAP·CypB and 1 μm cyclosporine A (orange).