<p>Changes of kinetic parameters for OPH-catalyzed hydrolysis of DFP after adding analog molecules of MEA, DEA and TEA.</p
Aminoalcohols have been addressed as activating buffers for alkaline phosphatase. However, there is ...
<p>Kinetic parameters of rOs1BGlu4 in the hydrolysis of <i>p</i>NP glycosides and oligosaccharides.<...
<p>Minimum three-step mechanism underlying the pre steady-state and steady-state parameters for the ...
<p>Kinetic parameters of OPH mutants in the DFP hydrolysis with or without triethanolamine (TEA).</p
<p>Kinetic parameters of wild-type OPH in the DFP hydrolysis in fluoride inhibition with or without ...
<p>The reaction was carried out in the presence of 100 μM ZnCl<sub>2</sub>, at pH 8.0 and 25°C. The ...
<p>The velocity (<i>V</i>) for OPH-catalyzed hydrolysis of DFP under 0 (○) and 300 mM (□) TEA condit...
<p>Apparent kinetic parameters for hydrolysis of chloropropionate substrates by wild type and mutant...
<p>The reaction was carried out in 0 mM (○), 100 mM (□), 200 mM (△), and 300 mM (▽) TEA-HCl buffer (...
<p>Kinetic parameters for the substrate hydrolysis by the wild-type and mutant Sfβgly.</p
<p>Kinetic parameters for the hydrolysis of the dipeptides AlaPro and AlaPro-NH<sub>2</sub> by wild-...
<p>Kinetic constants for the hydrolysis of pNPP are included for comparison.</p><p>Kinetic constants...
<p>The inhibition analysis of fluoride was performed at the increasing triethanolamine (TEA) concent...
<p>Kinetic rate constants of hydrolysis of Z-FR-MCA by rCPB2.8 in absence or in the presence of 40 µ...
<p>Each experiment was repeated three times.</p><p>Kinetic parameters for hydrolytic substrates of l...
Aminoalcohols have been addressed as activating buffers for alkaline phosphatase. However, there is ...
<p>Kinetic parameters of rOs1BGlu4 in the hydrolysis of <i>p</i>NP glycosides and oligosaccharides.<...
<p>Minimum three-step mechanism underlying the pre steady-state and steady-state parameters for the ...
<p>Kinetic parameters of OPH mutants in the DFP hydrolysis with or without triethanolamine (TEA).</p
<p>Kinetic parameters of wild-type OPH in the DFP hydrolysis in fluoride inhibition with or without ...
<p>The reaction was carried out in the presence of 100 μM ZnCl<sub>2</sub>, at pH 8.0 and 25°C. The ...
<p>The velocity (<i>V</i>) for OPH-catalyzed hydrolysis of DFP under 0 (○) and 300 mM (□) TEA condit...
<p>Apparent kinetic parameters for hydrolysis of chloropropionate substrates by wild type and mutant...
<p>The reaction was carried out in 0 mM (○), 100 mM (□), 200 mM (△), and 300 mM (▽) TEA-HCl buffer (...
<p>Kinetic parameters for the substrate hydrolysis by the wild-type and mutant Sfβgly.</p
<p>Kinetic parameters for the hydrolysis of the dipeptides AlaPro and AlaPro-NH<sub>2</sub> by wild-...
<p>Kinetic constants for the hydrolysis of pNPP are included for comparison.</p><p>Kinetic constants...
<p>The inhibition analysis of fluoride was performed at the increasing triethanolamine (TEA) concent...
<p>Kinetic rate constants of hydrolysis of Z-FR-MCA by rCPB2.8 in absence or in the presence of 40 µ...
<p>Each experiment was repeated three times.</p><p>Kinetic parameters for hydrolytic substrates of l...
Aminoalcohols have been addressed as activating buffers for alkaline phosphatase. However, there is ...
<p>Kinetic parameters of rOs1BGlu4 in the hydrolysis of <i>p</i>NP glycosides and oligosaccharides.<...
<p>Minimum three-step mechanism underlying the pre steady-state and steady-state parameters for the ...
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