There has been increasing interest in issues of initial rates , not necessarily at times approximately equal to zero but for all times referring to different durations of assay. This is with a view to addressing the problem of accurate kinetic parameters that are vital in most industrial, medical, and scientific research. The kinetic parameters must be addressed in the context of definite quasi-steady-state assumptions, as regularly advocated in the literature . Known or unknown to the advocates of single turnover catalytic events, the underlying assumption is the reverse quasi-steady-state assumption based on the premise that in such assays [E0] ≫ [S0] . The essence is to pursue a single-turnover approach and thereby prevent catalytic cycling in order to measure chemical steps. To isolate events at the active site of the enzyme without catalytic cycling, single-turnover conditions are utilized so that all of the substrate will participate in the 'single-turnover' . Against these backdrops, unlike in the literature, the goal of this study is to contrast turnover number, turnover frequency, number of catalytic cycles, and frequency of catalytic cycles per unit time with each other. The main objectives are the derivation of equations for the determination of all parameters, the evaluation of the equations with experimental data, and the determination of the number of substrate fragments per molecule of the enzyme. Here, a molar mass-based and a double reciprocal plot model linked to the number of catalytic cycles are essential for the primary determination of the number of catalytic cycles per a given number of moles of the enzyme in a reaction mixture.