2,3-Bisphosphoglyceric acid

• 2,3- BPG
• 2,3- diphosphoglycerate (deprecated)
• 2,3- DPG (deprecated)

Fixed

Slightly soluble in water: 10.2 g · l-1 (20 ° C)

Template: Infobox chemical / molecular formula search available

2,3- bisphosphoglycerate (2,3- BPG ), called 2,3- diphosphoglycerate outdated (2,3- DPG ) is a C3 body, each with a charged phosphate group at the second and third carbon atom. It further has the first carbon atom to a charged carboxyl group. Overall, it is (blood) charged five times in a negative solution. It is in the Rapoport - Luebering cycle, formed a minor route of glycolysis, from 1,3- bisphosphoglycerate using the Bisphosphoglyceratmutase. Under physiological conditions, about 20 percent of the costs incurred during the glycolysis of erythrocytes 1,3 - Bisphosphoglycerats be converted to 2,3- BPG, the remaining 80 percent through the main path via 3-phosphoglycerate in glycolysis.

2,3- BPG plays a crucial role in the regulation of hemoglobin (Hb). Binds it to the tense - form of hemoglobin ( deoxyhemoglobin ), this form is stabilized and can not pass into the oxygen affinity R-form. With bound 2,3 -DPG hemoglobin releases oxygen from even at a higher partial pressure. 2,3- BPG complicates further oxygenation of hemoglobin and facilitates delivery of oxygen bound to Hb. So that the balance of the oxygen binding curve ( HbO2 ↔ deoxy- Hb) is to the right, i.e., shifted to the side of the deoxy -Hb. Thus it is plausible that more oxygen can be delivered at a relatively reduced oxygen consumption. The phenomenon of rightward shift of the oxygen dissociation curve has practical consequences for mountain climbing and scuba diving. In high-altitude training this fact is used to let the first rise 2,3- BPG value whereby EPO mediated increased erythropoiesis is achieved.

2,3 -DPG in stored blood must be replaced with an analog such as inosine or glucose because it is unstable and rapidly decomposes. In the body, it is constantly synthesized new. The gamma -globin of fetal hemoglobin ( HbF ) has a lower affinity for 2,3- BPG. Thus ( HbA ) is increased compared to adult hemoglobin, the affinity of fetal hemoglobin for oxygen. Which enables easy transfer of oxygen from the mother to the fetus.

The arthropods have as respiratory pigment hemocyanin. Here, the lactate assumes the 2,3- BPG function and results in a displacement of the central portion of the oxygen- dissociation curve to the right.