<p>Lineweaver-Burk plots for urea (A) and GdnHCl (B). (C–D) The secondary plots of slope and y-intercept <i>versus</i> [urea] and [GdnHCl], respectively.</p
<p>Reciprocal initial velocities (Fig. 2) for two substrate conentrations were replotted against inh...
<p>(<b>A</b>) Inhibition potencies of the candidate compounds. The magnitudes of inhibition by compo...
The urease-catalyzed hydrolysis of urea has been found to be competitively inhibited by phosphate at...
<p>The inhibition and inactivation kinetic parameters of PTPase in the presence of urea and GdnHCl.<...
<p>Lineweaver-Burk double-reciprocal plots representing inhibitory profiles of compounds KuwE, PirII...
<p>The inactivation rate constants and residual activity of PTPase in the presence of different conc...
<p>(A) Urea concentrations for the labels 1–9 were 0, 1, 2, 3, 4, 5, 6, 7 and 8 M, respectively. (B)...
<p>Lineweaver-Burk plots of the inhibition kinetics of catechin and PCG against α-glucosidase.</p
<p>N, I, I* and D represent native state, partially active intermediate state, inactive intermediate...
<p>The concentrations of both ureases were 0.25 mg/mL. Data were expressed as means ± SD from three ...
<p>(<b>A</b>) Inhibition by Mg·AMP with Mg·ADP as variable substrate. Measurements were assayed at f...
<p>Compounds that shows inhibition of PTP1B at 1.25 μM concentration in <i>in vitro</i> assays.</p
<p>The two panels show representative plots of 1/<i>v</i> vs. 1/[NADH] (<b>A</b>) and 1/<i>v</i> vs....
We describe a fixed-time-interval, kinetic inhibition method, with use of a competitive inhibitor (0...
<p>The K<sub><b>i</b></sub> values represent the mean of two independent experiments; standard devia...
<p>Reciprocal initial velocities (Fig. 2) for two substrate conentrations were replotted against inh...
<p>(<b>A</b>) Inhibition potencies of the candidate compounds. The magnitudes of inhibition by compo...
The urease-catalyzed hydrolysis of urea has been found to be competitively inhibited by phosphate at...
<p>The inhibition and inactivation kinetic parameters of PTPase in the presence of urea and GdnHCl.<...
<p>Lineweaver-Burk double-reciprocal plots representing inhibitory profiles of compounds KuwE, PirII...
<p>The inactivation rate constants and residual activity of PTPase in the presence of different conc...
<p>(A) Urea concentrations for the labels 1–9 were 0, 1, 2, 3, 4, 5, 6, 7 and 8 M, respectively. (B)...
<p>Lineweaver-Burk plots of the inhibition kinetics of catechin and PCG against α-glucosidase.</p
<p>N, I, I* and D represent native state, partially active intermediate state, inactive intermediate...
<p>The concentrations of both ureases were 0.25 mg/mL. Data were expressed as means ± SD from three ...
<p>(<b>A</b>) Inhibition by Mg·AMP with Mg·ADP as variable substrate. Measurements were assayed at f...
<p>Compounds that shows inhibition of PTP1B at 1.25 μM concentration in <i>in vitro</i> assays.</p
<p>The two panels show representative plots of 1/<i>v</i> vs. 1/[NADH] (<b>A</b>) and 1/<i>v</i> vs....
We describe a fixed-time-interval, kinetic inhibition method, with use of a competitive inhibitor (0...
<p>The K<sub><b>i</b></sub> values represent the mean of two independent experiments; standard devia...
<p>Reciprocal initial velocities (Fig. 2) for two substrate conentrations were replotted against inh...
<p>(<b>A</b>) Inhibition potencies of the candidate compounds. The magnitudes of inhibition by compo...
The urease-catalyzed hydrolysis of urea has been found to be competitively inhibited by phosphate at...
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