American Society of Hematology

Figure 5.

The influence of the activating mAbs on the kinetics of VWF96 proteolysis by ADAMTS13. The initial rates (nMs−1) of VWF96 proteolysis (per nanomole of ADAMTS13(V5-6xHis)) in the absence of mAbs (orange) (A) or in the presence of the activating mAbs 17G2 (blue) (B) or 3E4 (red) (C) were plotted as a function of VWF96 concentration (0-25 μM) and fitted to the Michaelis Menten equation, for independent derivation of the kcat and Km of proteolysis. (D) The fitted Michaelis Menten plots for VWF96 proteolysis in the absence (orange, dashed line) or presence of the activating mAbs 3E4 (red, solid line) and 17G2 (blue, solid line), are plotted on the same axes.

The influence of the activating mAbs on the kinetics of VWF96 proteolysis by ADAMTS13. The initial rates (nMs⁻¹) of VWF96 proteolysis (per nanomole of ADAMTS13_(V5-6xHis)) in the absence of mAbs (orange) (A) or in the presence of the activating mAbs 17G2 (blue) (B) or 3E4 (red) (C) were plotted as a function of VWF96 concentration (0-25 μM) and fitted to the Michaelis Menten equation, for independent derivation of the k_cat and K_m of proteolysis. (D) The fitted Michaelis Menten plots for VWF96 proteolysis in the absence (orange, dashed line) or presence of the activating mAbs 3E4 (red, solid line) and 17G2 (blue, solid line), are plotted on the same axes.

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