AbstractThe kinetics of complexing inactivation at identical enzyme and inhibitor concentrations were analyzed and the equations of product generation were derived when the free enzyme concentration is great, larger or smaller than the dissociation constant of inhibitor, KI. The kinetic constants can be obtained by fitting the derived equations to the progress curve. Numerical examples show that this method is valid and gives satisfactory results
The maximum velocity (Vmax) of catalysis and the substrate concentration ([ST]) at half the Vmax, th...
Starting with the development of an enzymatic assay, where an enzyme in solution hydrolysed a solid-...
In this paper we study the model of the chemical reaction of fully competitive inhibition and determ...
AbstractThe kinetics of complexing inactivation at identical enzyme and inhibitor concentrations wer...
Enzyme inhibition by its substrate in excess, substrate inhibition, is one of the common deviations ...
The mathematics and geometry of the "kobs" method under the tight-binding experimental conditions, w...
Most general biochemistry textbooks present enzyme inhibition by showing how the basic Michaelis-Men...
AbstractThe extents to which different rate constants limit the steady-state rate of an isolated enz...
Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interaction...
factory ®t of more than one progress curve to the same A computer program with the code name DYNAFIT...
simple graphical method for the determination of reversible inhibition type,inhibitio constant(Ki) ...
<div><p>A difficulty associated with high throughput screening for enzyme inhibitors is to establish...
A difficulty associated with high throughput screening for enzyme inhibitors is to establish reactio...
The rate of product formation is an important measure of the speed of enzyme reactions. Classical st...
The Michaelis–Menten model of enzyme kinetic assumes the free ligand approximation, the steady-state...
The maximum velocity (Vmax) of catalysis and the substrate concentration ([ST]) at half the Vmax, th...
Starting with the development of an enzymatic assay, where an enzyme in solution hydrolysed a solid-...
In this paper we study the model of the chemical reaction of fully competitive inhibition and determ...
AbstractThe kinetics of complexing inactivation at identical enzyme and inhibitor concentrations wer...
Enzyme inhibition by its substrate in excess, substrate inhibition, is one of the common deviations ...
The mathematics and geometry of the "kobs" method under the tight-binding experimental conditions, w...
Most general biochemistry textbooks present enzyme inhibition by showing how the basic Michaelis-Men...
AbstractThe extents to which different rate constants limit the steady-state rate of an isolated enz...
Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interaction...
factory ®t of more than one progress curve to the same A computer program with the code name DYNAFIT...
simple graphical method for the determination of reversible inhibition type,inhibitio constant(Ki) ...
<div><p>A difficulty associated with high throughput screening for enzyme inhibitors is to establish...
A difficulty associated with high throughput screening for enzyme inhibitors is to establish reactio...
The rate of product formation is an important measure of the speed of enzyme reactions. Classical st...
The Michaelis–Menten model of enzyme kinetic assumes the free ligand approximation, the steady-state...
The maximum velocity (Vmax) of catalysis and the substrate concentration ([ST]) at half the Vmax, th...
Starting with the development of an enzymatic assay, where an enzyme in solution hydrolysed a solid-...
In this paper we study the model of the chemical reaction of fully competitive inhibition and determ...