Experimentally Induced Alterations in the Affinity of Hemoglobin for Oxygen. I. In Vitro Restoration of Erythrocyte 2,3-Diphosphoglycerate and Its Relationship to Erythrocyte Purine Nucleoside Phosphorylase Activity in a Variety of Species

The relationship between red cell purine nucleoside phosphorylase activity and the ability of stored erythrocytes to regenerate the organic phosphate 2,3-diphosphoglycerate was evaluated in man, monkey, rabbit, dog, cat, and rat. A linear relationship was observed between the activity of this enzyme and the in vitro regeneration of 2,3-diphosphoglycerate from a solution of inosine, pyruvate, and inorganic phosphate. These studies suggest that rabbit and monkey erythrocytes respond in a manner similar to that of human erythrocytes and, therefore, might be useful experimental models for the evaluation of pharmacologic methods for the in vivo alteration of the oxygen-hemoglobin equilibrium curve.