<p>Peroxidase assays were performed as described in Materials and Methods with the concentrations of all components except the peroxides (eight concentrations; 0–1 mM) held constant. To determine Michaelis constants, all reaction mixtures contained 50 mM sodium phosphate (pH 7.4), 50 mM NaCl, 1 mM DTPA (pH 7.4), 0.2 mM NADPH, 0.1 μM Ohr, and either the Lpd/SucB system (5 μM SucB and 40 μM Lpd), the LpdA system (40 μM), or the Trx system (5 μM TrxR and 40 μM Trx). The data represent the means obtained from three independent assays.</p><p>Kinetic constants for different Ohr substrates.</p
<p>The substrates H<sub>2</sub>O<sub>2</sub> (0.5 mM) and ABTS (0.5 mM) were mixed with various conc...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...
<p>Peroxidase assays were performed as described in Materials and Methods using fixed concentrations...
<p>Peroxide concentrations were determined at the indicated time points using the FOX assay describe...
<p>The steady-state kinetic parameters of the peroxidase reaction catalyzed by HRP, <i>Rd</i>. trHb ...
For some time now, there has been growing interest in pre-steady-state (PSS) kinetic parameters for ...
<p>The Michaelis–Menten plots for enzyme activity were generated in the presence of different concen...
<p>(<b>a</b>) The Michaelis-Menten plots of PrxQ activity versus different substrates by NADPH-coupl...
<p>The kinetic parameters <i>K</i>m and <i>V</i>max were determined by fitting the hydrolyzing rate ...
<p>A) Varied ATP concentrations in presence of 60 µM R5P. B) Varied R5P concentrations in presence o...
Abstract In the chapters dealing with enzyme reactions, the authors of all Biochemistry textbooks an...
<p>Apparent steady-state kinetic constants for <i>Mt</i>PRS, measured under standard assay condition...
<p>Michaelis-Menten plots of the initial rates of removal of H<sub>2</sub>O<sub>2</sub> (A), t-BOOH ...
Peroxidase enzymes oxidise phenolic compounds to produce free radicals which spontaneously polymeriz...
<p>The substrates H<sub>2</sub>O<sub>2</sub> (0.5 mM) and ABTS (0.5 mM) were mixed with various conc...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...
<p>Peroxidase assays were performed as described in Materials and Methods using fixed concentrations...
<p>Peroxide concentrations were determined at the indicated time points using the FOX assay describe...
<p>The steady-state kinetic parameters of the peroxidase reaction catalyzed by HRP, <i>Rd</i>. trHb ...
For some time now, there has been growing interest in pre-steady-state (PSS) kinetic parameters for ...
<p>The Michaelis–Menten plots for enzyme activity were generated in the presence of different concen...
<p>(<b>a</b>) The Michaelis-Menten plots of PrxQ activity versus different substrates by NADPH-coupl...
<p>The kinetic parameters <i>K</i>m and <i>V</i>max were determined by fitting the hydrolyzing rate ...
<p>A) Varied ATP concentrations in presence of 60 µM R5P. B) Varied R5P concentrations in presence o...
Abstract In the chapters dealing with enzyme reactions, the authors of all Biochemistry textbooks an...
<p>Apparent steady-state kinetic constants for <i>Mt</i>PRS, measured under standard assay condition...
<p>Michaelis-Menten plots of the initial rates of removal of H<sub>2</sub>O<sub>2</sub> (A), t-BOOH ...
Peroxidase enzymes oxidise phenolic compounds to produce free radicals which spontaneously polymeriz...
<p>The substrates H<sub>2</sub>O<sub>2</sub> (0.5 mM) and ABTS (0.5 mM) were mixed with various conc...
<p>Michaelis-Menten parameters from steady-state kinetics with 2-deoxy-d-ribose-5-phosphate (D5P) as...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...