An Analysis of Models of Cooperative Oxygen Binding by Hemoglobin

A New Model of Hemoglobin Oxygenation

“…It should also be noted that the equilibrium reaction constants of the above equation are apparent and it is not clear from them what the value of p 50 is [ 33 ]. As this equation consists of four components and is given by the same number of fitting coefficients ( K 1 – K 4 ), it is expected to have a higher approximation capability relative to the Hill and Bernard equations [ 25 ].…”

“…This model has a better approximation of experimental data on hemoglobin oxygenation relative to Hill’s equation and is comparable with Adair’s equation; however, it describes hemoglobin oxygenation at its initial stages worse than the latter. It should also be noted that there are several publications in which macromolecule-binding constants are also considered as functions of macromolecule filling by ligands [ 25 , 39 , 40 , 41 ].…”

“…We considered oxygenation characterized by p 50 and h as a function of oxygen partial pressure. Note that the very idea of such a dependence, in which macromolecule-binding constants are considered to be a function of macromolecule filling with ligands, is not new [ 25 , 39 , 40 , 41 ].…”

“…Previously, we proposed a mathematical model for hemoglobin oxygenation [ 25 , 26 ] and ascertained that our model fits better to experimental oxyhemoglobin dissociation curves when compared with the classical Hill equation and is comparable with the Adair equation (Adair–Klotz) [ 26 ]. However, for oxygen partial pressure levels below 3 mm Hg, the proposed equation is inferior to the Adair equation in accuracy approximation.…”