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. Author manuscript; available in PMC: 2010 Jul 7.
Published in final edited form as: Biochemistry. 2009 Jul 7;48(26):6268–6277. doi: 10.1021/bi9007287

Figure 2.

Figure 2

A) Residual PPIase activity of CypA (closed circles) and CypB (open triangles) by compound 1. B) Reversibility of CypA inhibition by compound 2 analyzed by dilution experiments. CypA (0.75 μM) and 2 (0.02 - 200 μM) were incubated for 30 min. After 1:375 dilution in 35 mM HEPES buffer pH 7.8, the PPIase activity was determined (bars) and compared with the PPIase activity of CypA at the indicated concentrations of compound 2. The PPIase activity of CypA completely recovered from the inhibited enzyme. The PPIase activity was measured in 35 mM HEPES buffer at pH 7.8 and 283 K using Suc-Ala-Ala-Pro-Phe-pNA as substrate. Each data point represents the mean of two measurements with a deviation less than 10 %.