Its synthesis and breakdown are, therefore, a way around a step of glycolysis, with the net expense of one ATP per molecule of 2,3-BPG generated as the high-energy carboxylic acid-phosphate mixed anhydride bond is cleaved by 2,3-BPG phosphatase.

There is a delicate balance between the need to generate ATP to support energy requirements for cell metabolism and the need to maintain appropriate oxygenation/deoxygenation status of hemoglobin.

It fits neatly into the cavity of the deoxy- conformation, exploiting the molecular symmetry and positive polarity by forming salt bridges with lysine and histidine residues in the β subunits of hemoglobin.

Increased binding affinity of fetal hemoglobin relative to HbA facilitates the passage of oxygen across the placental membrane from the mother to the fetus.

The result was that the hyperthyroidism modulates in vivo 2,3-BPG content in erythrocytes by changes in the expression of phosphoglycerate mutase (PGM) and 2,3-BPG synthase.

Physiologically, an increase in 2,3-BPG levels would be expected to counteract the hypoxia that is frequently observed in this process.

This is due to the procedure itself: mechanical stress on the erythrocytes is believed to cause the 2,3-BPG escape, which is then removed by hemodialysis.

The concentrations of calcium, phosphate, creatinine, urea and albumin did not correlate significantly with the total change in 2,3-BPG/Hb4 ratio.

However, the ratio sampled just before dialysis correlated significantly and positively with the total weekly dosage of erythropoietin (main hormone in erythrocyte formation) given to the patients.