The influence of sodium phosphate supplementation on VO2max, serum 2,3-diphosphoglycerate level and heart rate in off-road cyclists.
Effects of sodium phosphate loading on aerobic power and capacity in off road cyclists. Dempsey, J. With haemoglobin as with politics - should we shift right or left? Exercise-induced arterial hypoxemia. Dominelli, P. Influence of high affinity haemoglobin on the response to normoxic and hypoxic exercise. Duhm, J. On the mechanisms of the hypoxia-induced increase of 2,3-diphosphoglycerate in erythrocytes. Pflugers Arch.
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Management of acid-base disorders and pre-operative aklalinization of patients with sickle cell disease whould take account of this. It is known that anaesthesia alters the position of the oxyhaemoglobin dissociation curve, but it is thought that this is independent of any effects which anaesthetic agents may have on 2,3-DPG concentration.
During the T state to R state transition, the 2,3-bisphophoglycerate is released. It's vital to oxygen transfer, since the T state must be stabilized until the transition point. However, the T state is very unstable resulting for hemoglobin's affinity for oxygen and thus tries to bind to oxygen, disrupting the T state. Without 2,3-BPG, this stabilization cannot occur thanks to its inhibition abilities. The enzyme is used in the Embden-Meyerhof pathway of glycolysis in erythrocytes.
The pathway is the anaerobic metabolic pathway that converts glycogen to lactic acid in human muscle.
The effect of 2,3-bisphosphoglycerate is shown between the fetal red cells and the maternal red cells. The maternal red cells are able to bind 2,3-bisphosphoglycerate better than the fetal red cells.
Therefore the fetal red cells have a higher oxygen affinity which explains why oxygen flows from oxyhemoglobin to the fetal deoxyhemoglobin. Since the fetal red cells contain a higher oxygen affinity, it allows oxygen to be carried to the placenta. By selectively binding to deoxyhemoglobin, 2,3-BPG stabilizes the T state conformation, making it harder for oxygen to bind hemoglobin and more likely to be released to adjacent tissues. Conditions of low tissue oxygen concentration such as high altitude 2,3-BPG levels are higher in those acclimated to high altitudes , airway obstruction , or congestive heart failure will tend to cause RBCs to generate more 2,3-BPG in their effort to generate energy by allowing more oxygen to be released in tissues deprived of oxygen.
Ultimately, this mechanism increases oxygen release from RBCs under circumstances where it is needed most. This release is potentiated by the Bohr effect in tissues with high energetic demands. Interestingly, fetal hemoglobin HbF exhibits a low affinity for 2,3-BPG, resulting in a higher binding affinity for oxygen.
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