Crystal structure of human arginase I at 1.29-Å resolution and exploration of inhibition in the immune response

Di Costanzo et al. 10.1073/pnas.0504027102.

Supporting Figures

Files in this Data Supplement:

Fig. 6. Isothermal titration calorimetry of wild-type human arginase I-ABH complexation at 21°C. The area under each peak (Upper) is integrated and plotted against [ABH]/[arginase] (Lower). The solid line represents the nonlinear least-squares best fit of the experimental data and yields a dissociation constant K_d = 5.0 ± 1.0 nM with a molar binding stoichiometry of 2.20.

Supporting Figure 7

Fig. 7. Isothermal titration calorimetry of wild-type human arginase I-BEC complexation at 21°C. The area under each peak (Upper) is integrated and plotted against [BEC]/[arginase] (Lower). The solid line represents the nonlinear least-squares best fit of the experimental data and yields a dissociation constant K_d = 270 ± 50 nM with a molar binding stoichiometry of 2.08.