I. I. Udema

Where Initial rates are directly proportional to Substrate concentrations with Application in Molar-mass Determination, Zero-order Specificity constant is Inappropriate

The paper demonstrates that initial rate (vi) is not equal to Vmax[S0]/KM, confirms Kd is proportional to [E0], and shows the limited validity of sQSSA and rQSSA assumptions.

Alternative equations and "pseudo-statistical" approaches that enhance the precision of initial rates for the determination of kinetic parameters

This paper introduces new equations to correct initial rates in enzyme assays, improving the accuracy of Michaelis-Menten parameters compared to existing methods.

The life span of steps in the enzyme-catalyzed reaction, its implications, and matters of general interest

The paper derives equations to calculate the life span and first-order rate constants for key steps in enzyme-catalyzed reactions using mesophilic alpha-amylase and the Bernfeld assay method.

Directly and indirectly determinable rate constants in Michaelian enzyme-catalyzed reactions

The paper derives equations to calculate rate constants for enzyme-catalyzed reactions and quantifies specific rate constants for activation and deactivation of enzyme-substrate and enzyme-product complexes.

Derivation of Steady-State First-order Rate Constant Equations for Enzyme-Substrate Complex Dissociation, as well as Zero-order Rate Constant Equations in Relation to Background Assumptions

The paper challenges the classification of Vmax and KM as steady-state parameters by deriving new equations for first-order rate constants and analyzing assumptions in enzyme kinetics.