2,3-Diphosphoglycerate is a negative allosteric heterotropic effector of oxygen binding to haemoglobin. It modulates the oxygen affinity of haemoglobin, binding tightly to the deoxygenated form (T state) of the molecule, but poorly to the oxygenated or other ligand-bound forms. Binding occurs stereo-specifically within the central cavity of the haemoglobin tetramer. It stabilises deoxyhaemoglobin, favouring oxygen release. Each red blood cell contains 15 mmol/g 2,3-DPG (molar J
e ratio of 1:1 with haemoglobin). A polyanion, it forms 15% of the anionic content 3
o of red blood cell. One mole of 2,3-DPG binds to one mole of deoxyhaemoglobin. O
It is bound between the two beta subunits by ionic salt bridges. n
The rate of synthesis is controlled by the concentrations of unbound 1,3-DPG and 2,3-DPG (Rapoport-Luebering shuttle) Chronic hypoxia Prolonged exercise
Enzyme abnormalities of the red cells
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