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Area of ​​Expertise - biochemistry

2,3-Diphosphoglycerate (2,3-DPG) - referred to as 2,3-bisphosphoglycerate (2,3-BPG) according to the newer nomenclature - is a regulator of the oxygen binding to hemoglobin. 2,3-DPG binds non-covalently to deoxyhemoglobin, but not to oxyhemoglobin, reducing the oxygen affinity of hemoglobin by a factor of 26. This is noticeable in the oxygen dissociation curve as the curve shifts to the right.

The molar 2,3-DPG concentration in the erythrocytes is about the same as that of hemoglobin under normal conditions. This explains why (isolated) free hemoglobin in solution has a significantly higher oxygen affinity than the hemoglobin in erythrocytes. If the tissue is inadequately supplied with oxygen, the concentration of 2,3-DPG can adapt accordingly. When moving to higher altitudes, for example, the 2,3-DPG concentration is increased over time and thus the oxygen affinity of the hemoglobin is reduced, so that the oxygen can also be released from the erythrocytes in the tissue under these conditions.

Fetal hemoglobin can bind oxygen in the body significantly better than adult hemoglobin, which aids the transfer of oxygen from the maternal to the fetal bloodstream. In free form, however, fetal hemoglobin even has a slightly lower affinity. The 2,3-DPG is also responsible for this effect. This is because fetal deoxyhemoglobin binds the regulator far worse, resulting in better binding of oxygen.

Video: Biphosphoglycerate or diphosphoglycerate cycle in Red Blood Cell (August 2022).