To explain the kinetics of enzyme-substrate reactions, Michaelis and Menten (1913) came up with a mechanism, which uses an equilibrium assumption. Briggs and Haldane (1925), on the other hand, employed a steady-state assumption in place of the equilibrium assumption and came up with their own mechanism. In this work, the method outlined by Boudart (1968) for surface reaction was applied to mechanism of enzyme-substrate reactions. The Cramer’s rule was applied to solve the sets of algebraic equations obtained from the method. The results obtained are similar to those of Michaelis and Menten as well as those of Briggs and Haldane. This work shows the power of applied Mathematics to explain natural phenomena and attestation to the fact that en...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
For some time now, there has been growing interest in pre-steady-state (PSS) kinetic parameters for ...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The use of the classic Henry-Michaelis-Menten (HMM) model (or simply, Michaelis-Menten model) to stu...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for ...
The nonlinear dependence of the rate expressions associated with enzymecatalysed reactions on the c...
Many in vivo enzymatic processes, such as those of the tissue factor pathway of blood coagulation, o...
To achieve transition from lab scale enzyme studies to industrial applications, understanding of enz...
This dissertation contains several enzyme kinetics studies, each demonstrating the importance of dim...
The rate of product formation is an important measure of the speed of enzyme reactions. Classical st...
The application of the quasi-steady-state approximation (QSSA) in biochemical kinetics allows the re...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
For some time now, there has been growing interest in pre-steady-state (PSS) kinetic parameters for ...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The use of the classic Henry-Michaelis-Menten (HMM) model (or simply, Michaelis-Menten model) to stu...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for ...
The nonlinear dependence of the rate expressions associated with enzymecatalysed reactions on the c...
Many in vivo enzymatic processes, such as those of the tissue factor pathway of blood coagulation, o...
To achieve transition from lab scale enzyme studies to industrial applications, understanding of enz...
This dissertation contains several enzyme kinetics studies, each demonstrating the importance of dim...
The rate of product formation is an important measure of the speed of enzyme reactions. Classical st...
The application of the quasi-steady-state approximation (QSSA) in biochemical kinetics allows the re...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
For some time now, there has been growing interest in pre-steady-state (PSS) kinetic parameters for ...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...