Purification and functional properties of the hemoglobin components from the rat (Wistar).

Homogeneous components of Wistar rat hemoglobin have been isolated and characterized from the molecular and functional point of view. The O2 equilibrium behaviour of the three main components (HbII, HbIII, HbIVA) has been investigated as a function of pH and organic phosphate concentration. The ligand-binding kinetics of the isolated components have been also studied and are fully consistent with their equilibrium behaviour. It should be remarked that the choice of the system was governed largely by the ability of rat hemoglobins to crystallize very quickly. This almost unique molecular property together with the complete reversibility of the process may allow information to be obtained on the thermodynamics of ligand-linked phase changes.