Abstract
The apparent binding constant (K i) and the first order rate constant of inactivation (k 3) have been obtained for EP-475 inhibition of papain at partially saturating concentrations of inhibitor and various substrate concentrations by global analysis of the data. The value of k 3 (k 3 = 0.71 ± 0.25 s −1) is larger whereas K i (2.4 ± 0.91 μM) is comparable to or higher than those values for most nucleofuge methylketone inhibitors.
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