Fig. 4: dasTMPRSS2 displays robust in vitro peptidase activity.
From: Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation

a, The generic Boc-Gln-Ala-Arg-AMC fluorogenic peptide substrate is efficiently cleaved by 3.4 nM dasTMPRSS2 in Assay Buffer pH 8.0. Representative progress curves are shown in technical duplicate (n = 2) with datapoints shown as mean values ± s.d. b, Michaelis–Menten plot of initial reaction velocities for kinetic parameter estimation after curve fitting in GraphPad. Each reaction velocity was tabulated in technical quadruplet (n = 4) and datapoints are shown as mean values ± s.d. c, Relative peptidase activity (normalized to Assay Buffer; 25 mM Tris pH 8.0, 75 mM NaCl, 2 mM CaCl2) calculated from initial reaction velocities under Tris pH 8.0 buffering conditions with varying concentrations of NaCl, CaCl2, EDTA and DMSO. Activity was measured in technical triplicate (n = 3) and data are shown as mean values ± s.d. No statistically significant differences from mean peptidase activity in Assay buffer were found (denoted as NS) in the indicated buffering conditions as determined by one-way analysis of variance for n = 3 biologically independent samples examined over one independent experiment.