Background: Previous research has shown that the intrinsic reverse (backward) and forward rate constants are larger than the effective or apparent rate constants for the formation and dissociation of an enzyme-substrate complex (ES). It is speculated that such intrinsic rate cons...
Open access
Research Article10.9734/ajocs/2022/v12i3219
Objectives: This research was undertaken to determine the non–equilibrium binding energy by calculation after substituting experimental data into derived equations, present its role distinct from energy associated with activated enzyme–substrate (ES) complex and ultimately elucid...
Open access
Research Article10.9734/ajocs/2020/v8i319044
Background: There had always been a spirited effort in understanding the transport of air or molecular oxygen plus other gases from alveolar air space into the pulmonary capillaries and from the latter back into the former using mathematical models; the determination of the numbe...
Open access
Research Article10.9734/ajob/2020/v10i130098
Background: There is a need for equations with which to calculate the intrinsic rate constants that can further characterise enzyme catalysed reactions despite what seems to be conventional differences in methodology in the literature. Methods: Theoretical, experimental (Bernfeld...
Open access
Research Article10.9734/ajocs/2020/v8i219037
Aims: The aims of the research were 1), to derive simple equations that can be used to determine mass concentration of reaction mixture components, and 2), to determine the mass concentration of free substrate, total mass concentration of substrate involved in enzyme-substrate co...
Open access
Research Article10.9734/IJBCRR/2017/35040
Aims: i) To show that attractive electrostatic interaction is essential to stable enzyme-substrate formation, ii) to determine the minimum interparticle distance for maximum attractive interaction, iii) to determine the duration and the velocity of transit before enzyme substrate...
Open access
Research Article10.9734/AIR/2017/32676
Aims: 1) To formulate models based on defined principle for the application of Fitter’s model and 2) ultimately show that there are changes in the radius of an enzyme in solution and consequently conformational entropy change with temperature before and during catalytic activity....
Open access
Research Article10.9734/IJBCRR/2017/31097
Aims: The objectives of the research were (i) to show that the mass concentration, molar mass of one-active site enzyme, and consequently, the type of human salivary alpha amylase (HSαA), can be determined using kinetic parameter dependent model, (ii) to show that the free energy...
Open access
Research Article10.9734/JSRR/2016/29395