Role and induction of 2,3-bisphosphoglycerate synthase.

2,3-Bisphosphoglycerate accumulates in mammalian erythrocytes, where it facilitates the supply of oxygen to the tissues by binding to hemoglobin. Regulatory properties of 2,3-bisphosphoglycerate synthase and phosphatase are discussed. The 2,3-bisphosphoglycerate concentration was shown to rise linearly along with the hemoglobin level during erythroid differentiation. The accumulation of 2,3-bisphosphoglycerate was primarily attributable to an increase in 2,3-bisphosphoglycerate synthase. Antibody-binding studies showed that the increased activity is achieved solely through an increase in the amount of enzyme. It was shown that 2,3-bisphosphoglycerate synthase was synthesized in nucleated erythroid precursor cells and also in anucleated reticulocytes. The mRNA of this protein appears to be fairly stable in reticulocytes. Coordinate expression of hemoglobin and 2,3-bisphosphoglycerate synthase was found during dimethylsulfoxide-induced differentiation of Friend erythroleukemia cells. 2,3-Bisphosphoglycerate rose concomitantly.