How does 2 3 bpg work

Diagnostic studies for 2,3-Bisphosphoglycerate. Treatment of 2,3-Bisphosphoglycerate. CME Programs on 2,3-Bisphosphoglycerate.

Patents on 2,3-Bisphosphoglycerate. List of terms related to 2,3-Bisphosphoglycerate. Editor-In-Chief: C. Michael Gibson, M. It binds with greater affinity to deoxygenated hemoglobin e. In bonding to partially deoxygenated hemoglobin it allosterically upregulates the release of the remaining oxygen molecules bound to the hemoglobin, thus enhancing the ability of RBCs to release oxygen near tissues that need it most. Its function was discovered in by Reinhold Benesch and Ruth Benesch.

It is broken down by a phosphatase to form 3-phosphoglycerate. Its synthesis and breakdown are therefore a way around a step of glycolysis. When 2,3-BPG binds deoxyhemoglobin, it acts to stabilize the low oxygen affinity state T state of the oxygen carrier. It fits neatly into the cavity of the deoxy- conformation, exploiting the molecular symmetry and positive polarity by forming salt bridges with lysine and histidine residues in the four subunits of hemoglobin.

The R state, with oxygen bound to a heme group, has a different conformation and does not allow this interaction. 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. Template:WikiDoc Sources. Biochem Biophys Res Commun. Respiratory system , physiology : respiratory physiology.

Categories : Pages with citations using unsupported parameters Organophosphates Physiology. Cookies help us deliver our services. By using our services, you agree to our use of cookies. Namespaces Home Page Discussion. Interaction of the effects of pH, Pco2, temperature and 2,3-DPG on the oxyhaemoglobin dissociation curve are discussed. The role of 2,3-DPG in the intraerythrocytic adaptation to various types of hypoxaemia is described. The increased oxygen affinity of blood stored in acid-citrate-dextrose ACD solution has been shown to be due to the decrease in the concentration of 2,3-DPG which occurs during storage.

Methods of maintaining the concentration of 2,3-DPG in stored blood are described. The clinical implication of transfusion of elderly people, anaemic or pregnant patients with ACD stored blood to anaesthetically and surgically acceptable haemoglobin concentrations are discussed. Hypophosphataemia in association with parenteral feeding reduces 2,3-DPG concentration and so increases oxygen affinity.

Disorders of acid-base balance effect oxygen affinity not only by the direct effect of pH on the oxyhaemoglobin dissociation curve but by its control of 2,3-DPG metabolism.