The Hemoglobin Function of Blood Stored at 4°C

Abstract

It is appropriate that this First International Conference on Red Cell Metabolism and Function is dedicated to A. C. This investigator noted that a slow moving electrophoretic component (B) decreased at the same rate as red cell organic phosphate concentrations during the storage of blood (Berry and Chanutin, 1958). This was assumed to be a hemoglobin-organic phosphate complex. After Bartlett and Barnett (1960) found that 2, 3-DPG became rapidly depleted in ACD-stored blood, component B was found to be composed chiefly of DPG and ATP (Sugita and Chanutin, 1963; Chanutin and Curnish, 1964, 1965a). Further work showed that this complex was capable of decreasing the affinity of oxygen to hemoglobin (Chanutin, 1966). Since DPG is present in large amounts in the red cell, it was clear that the Hb-DPG complex is important for decreasing the affinity of O₂ to hemoglobin. This effect was confirmed (Chanutin and Curnish, 1967; Benesch and Benesch, 1967), and recent studies have shown binding of 2, 3-DPG to both oxyhemoglobin and deoxyhemoglobin, using equilibrium dialysis (Chanutin and Hermann, 1969) and ultracentrifugation (de Verdier and Garby, 1969).