<p>Michaelis-Menten plots of the initial reaction velocities (v) for different concentrations of substrate are shown. Different amounts of AtAPY1-GFP enzyme were used in (A), (B) and (C) as a result of different starting material. The enzyme velocities were determined by the continuous assay. For each substrate concentration, the mean velocity calculated from two parallel reactions was plotted. The initial velocities were linear over time for ≥ 30 min. Each initial velocity was determined from a minimum of 24 data points from this linear phase. The error bars represent the standard deviations of the velocity means. The data set is representative of six (A, B) and three experiments (C), respectively.</p
Enzyme kinetics were determined with 0.25 mg mL−1 enzyme. The concentration of substrate ranged from...
AbstractParameters often are tuned with metabolite concentration time series data to build a dynamic...
<p>A. Plot of the initial velocity <i>versus</i> the GMP concentration in the presence of 200 μM NAD...
<p>The plots show the dependence of initial velocity upon substrate concentration for the following ...
A new method is described for estimating initial velocities of enzyme-catalysed reactions. It is sim...
<p>Activities of enzymes were calculated using Lineweaver-Burk plots. MIPS assays were done at each ...
Measuring the initial velocity is difficult in some enzyme assays where a significant fraction of th...
<p>Enzyme activities were determined in the presence of 3 mM UDP using the discontinuous apyrase act...
Abstract In the chapters dealing with enzyme reactions, the authors of all Biochemistry textbooks an...
Most methods for studying the kinetic properties of an enzyme involve the determination of initial v...
<p>The Michaelis–Menten plots for enzyme activity were generated in the presence of different concen...
The statistical implications of the direct linear plot for enzyme kinetic data, described in the pre...
<p>To determine the scope of initial reaction velocity, enzymatic reactions (100 µl) containing 0.5 ...
<p>a b Double reciprocal plots of the relationship between the concentration of peptide substrate an...
The nature of experimental error in the determination of initial velocities of enzyme-catalysed reac...
Enzyme kinetics were determined with 0.25 mg mL−1 enzyme. The concentration of substrate ranged from...
AbstractParameters often are tuned with metabolite concentration time series data to build a dynamic...
<p>A. Plot of the initial velocity <i>versus</i> the GMP concentration in the presence of 200 μM NAD...
<p>The plots show the dependence of initial velocity upon substrate concentration for the following ...
A new method is described for estimating initial velocities of enzyme-catalysed reactions. It is sim...
<p>Activities of enzymes were calculated using Lineweaver-Burk plots. MIPS assays were done at each ...
Measuring the initial velocity is difficult in some enzyme assays where a significant fraction of th...
<p>Enzyme activities were determined in the presence of 3 mM UDP using the discontinuous apyrase act...
Abstract In the chapters dealing with enzyme reactions, the authors of all Biochemistry textbooks an...
Most methods for studying the kinetic properties of an enzyme involve the determination of initial v...
<p>The Michaelis–Menten plots for enzyme activity were generated in the presence of different concen...
The statistical implications of the direct linear plot for enzyme kinetic data, described in the pre...
<p>To determine the scope of initial reaction velocity, enzymatic reactions (100 µl) containing 0.5 ...
<p>a b Double reciprocal plots of the relationship between the concentration of peptide substrate an...
The nature of experimental error in the determination of initial velocities of enzyme-catalysed reac...
Enzyme kinetics were determined with 0.25 mg mL−1 enzyme. The concentration of substrate ranged from...
AbstractParameters often are tuned with metabolite concentration time series data to build a dynamic...
<p>A. Plot of the initial velocity <i>versus</i> the GMP concentration in the presence of 200 μM NAD...