2,3-DPG

2,3-DPG

An inorganic phosphate produced in red cells by the Rapoport-Luebering shunt; 2,3-DPG binds to the beta chain of reduced haemoglobin (Hb), lowering Hb's affinity for O2 and by extension, facilitating O2 release to tissues, causing a "right shift" of the O2 dissociation curve. 2,3-DPG further shifts the curve to the right by lowering the red cells' pH, When transfused, red cells regain 50% of the 2,3-DPG within 3–8 hours and 100% within 24 hours.
Increased DPG High altitude, anaemia, chronic hypoxia, hyperthyroidism, chronic alkalosis
Decreased DPG Storage of blood, hypothyroidism, hypophosphatemia, acidosis

2,3-diphosphoglycerate

(dī″fŏs-fō-glĭs′ĕr-āt″),

2,3-DPG

An organic phosphate in red blood cells that alters the affinity of hemoglobin for oxygen. Blood cells stored in a blood bank lose 2,3-diphosphoglycerate, but once they are infused, the substance is resynthesized or reactivated.

2,3-DPG

2,3-diphosphoglycerate
References in periodicals archive ?
Fetal hyperglycemia, fetal hyperinsulinemia, as well as decreased 2,3-DPG levels causing an increased affinity of maternal hemoglobin for oxygen can lead to lactic acidosis and hypoxia in the fetus (2),(5).
Some research support this hypothesis, while other studies do not show significant changes in the level of erythrocyte 2,3-DPG following sodium phosphate supplementation (Bredle et al.
Venous blood samples were drawn, before and after the exercise protocol to determine hemoglobin concentration (Hb), haematocrit value (Hct), number of erythrocytes (RBC), concentration of non-organic phosphates, serum calcium concentration, and the level of 2,3-DPG.
These blood samples were necessary for hematological variables which were used to calculate 2,3-DPG concentration per erythrocyte.
But stored blood loses a chemical called 2,3-DPG (for 2,3 diphosphoglycerate) that facilitates the unloading of oxygen from hemoglobin molecules on red blood cells.
These findings suggest that the absence of proline [beta]5 slightly affects the spatial positions of Val at NA1 and His at NA2 and indirectly affects the off-loading of 2,3-DPG as observed in Hb Warwickshire.
It exhibits normal oxygen affinity with normal cooperativity, Bohr effect, and 2,3-DPG interactions.
Therefore, the change in off-loading of 2,3-DPG in the case of this Hb variant could be attributable to the introduction of the positively charged arginine; although according to Wilson et al.
This increase of the 2,3-DPG concentration may be related to the chronic obstructive pulmonary disease and hyperthyroidism diagnosed in our patients.
Another approach involves covalently linking pyridoxal phosphate to the 2,3-DPG site [3].
2] affinity is not 2,3-DPG dependent but rather Cl- dependent [53].
Hb Source Modification Company Bovine Glutaraldehyde polymerization Biopure Bovine Polyethylene glycol polymerizat Enzon Bovine O-Raffinose cross-linked Hemosol Expired human Dibromosalicylate bisfumarate Baxter RBC Cross-linked [alpha] chains Expired human Gluteraldehyde polymerization Northfield Labs RBC Pyridoxylated 2,3-DPG site Recombinant human Covalent [alpha] chain dimers Somatogen Hb Presbyterian