Hemoglobins 2,3-diphosphoglycerate binding

Diphosphoglycerate A compound in red blood cells that affects oxygen binding to and release from hemoglobin. 

Hemoglobin s dioxygen binding is regulated by local concentrations of H+ (known as the Bohr effect), CO2 concentration, and organic phosphates such as diphosphoglycerate (DPG), whose structure is shown in Figure 4.2.17... 

Figure 10.11 Binding of 2,3-diphosphoglycerate (DPG) between the f3 chains in the central cavity of human hemoglobin. [From A. Amone and M. F. Perutz, Nature, Land. 249, 34 (1974).]...

The compound 2,3-bisphosphoglycerate (BPG, also known as 2,3-diphosphoglycerate or DPG) is produced within the red blood cell of many animal species, and acts to modify the oxygen binding affinity of hemoglobin ... 

Figure 28-19 Three compounds designed by Beddell and coworkers to mimic the binding of 2.3-diphosphoglycerate (DPG) (2) to hemoglobin.

In view of the known binding capacity of deoxygenated hemoglobin for 2,3-diphosphoglyceric acid (2,3-DPG) and adenine nucleoti-des it appeared likely that the inhibitory action of these effectors and accordingly the Pi requirement for the synthesis of PRPP in RBC would be considerably diminished under anaerobic conditions. This prediction was borne out by the data presented in Fig. 

Nelson, D. P., Miller, W. D., and Kiesow, L. A., 1974, Calorimetric studies of hemoglobin function, the binding of 2,3-diphosphoglycerate and inositol hexaphosphate to human hemoglobin A, J. Biol. Chem. 249 4770. 

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