We construct efficient designs for the Michaelis-Menten enzyme kinetic model capable of checking model assumption. An extended model, called EMAX model is also considered for this purpose. This model is widely used in pharmacokinetics and reduces to the MichaelisMenten model for a specific choice of the parameter setting. Our strategy is to find efficient designs for estimating the parameters i...

Often the Michaelis constant of an enzyme will be determined several times. This may be done for various reasons such as ensuring reproducibility, comparing different enzyme preparations, or examining the effects of variations in experimental conditions. In these circumstances, two questions arise. First, how can the various estimates of the Michaelis constant be compared to determine whether t...

In most of the real life problems, we encounter with nonlinear differential equations. Problems are made more understandable by modeling them these this way, it becomes easier to interpret problems and reach results. 1913, basic enzymatic reaction model introduced Michaelis Menten describe enzyme processes is an example equation. This one simplest best-known approaches mechanisms used enzyme-ca...

The basis of enzyme kinetic modelling was established during the early 1900’s when the work of Leonor Michaelis and Maud Menten produced a pseudo-steady state equation linking enzymatic catalytic rate to substrate concentration (Michaelis & Menten, 1913). Building from the Michaelis-Menten equation, other equations used to describe the effects of modifiers of enzymatic activity were developed b...

The electrocatalytic oxidation of vitamin B6 (pyridoxine hydrochloride) was demonstrated on a Nafion/lead ruthenate pyrochlore modified electrode (designated as NCME) by cyclic voltammetry. The catalytic activity of vitamin B6 was explored in terms of the higher oxidation state of ruthenium species, i.e., Py-Ru/Ru in the pyrochlore network (Py). The mediated mechanism was derived by Michaelis-M...