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  2. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygen–hemoglobin...

    2,3-Bisphosphoglycerate or 2,3-BPG (formerly named 2,3-diphosphoglycerate or 2,3-DPG) is an organophosphate formed in red blood cells during glycolysis and is the conjugate base of 2,3-bisphosphoglyceric acid.

  3. 2,3-Bisphosphoglyceric acid - Wikipedia

    en.wikipedia.org/wiki/2,3-bisphosphoglyceric_acid

    2,3-BPG is formed from 1,3-BPG by the enzyme BPG mutase.It can then be broken down by 2,3-BPG phosphatase to form 3-phosphoglycerate.Its synthesis and breakdown are, therefore, a way around a step of glycolysis, with the net expense of one ATP per molecule of 2,3-BPG generated as the high-energy carboxylic acid-phosphate mixed anhydride bond is cleaved by 2,3-BPG phosphatase.

  4. Packed red blood cells - Wikipedia

    en.wikipedia.org/wiki/Packed_red_blood_cells

    If a patient is stable and has a haematinic deficiency, they should be treated for the deficiency (iron deficiency, B 12 deficiency, or folate deficiency) rather than being given a red blood cell transfusion. [3] [4] In adults, blood transfusion is typically recommended when hemoglobin levels are below 70 g/L (7 g/dL) in those who have stable ...

  5. Luebering–Rapoport pathway - Wikipedia

    en.wikipedia.org/wiki/Luebering–Rapoport_pathway

    In biochemistry, the Luebering–Rapoport pathway (also called the Luebering–Rapoport shunt) is a metabolic pathway in mature erythrocytes involving the formation of 2,3-bisphosphoglycerate (2,3-BPG), which regulates oxygen release from hemoglobin and delivery to tissues. 2,3-BPG, the reaction product of the Luebering–Rapoport pathway was first described and isolated in 1925 by the ...

  6. Pyruvate kinase deficiency - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_kinase_deficiency

    The level of 2,3-bisphosphoglycerate is elevated: 1,3-bisphosphoglycerate, a precursor of phosphoenolpyruvate which is the substrate for Pyruvate kinase, is increased and so the Luebering-Rapoport pathway is overactivated. This led to a rightward shift in the oxygen dissociation curve of hemoglobin (i.e. it decreases the hemoglobin affinity for ...

  7. Fetal hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Fetal_hemoglobin

    One of the molecules is 2,3-bisphosphoglycerate (2,3-BPG) and it enhances hemoglobin's ability to release oxygen. [13] 2,3-BPG interacts much more with hemoglobin A than hemoglobin F. This is because the adult β subunit has more positive charges than the fetal γ subunit, which attract the negative charges from 2,3-BPG.

  8. Bisphosphoglycerate mutase - Wikipedia

    en.wikipedia.org/wiki/Bisphosphoglycerate_mutase

    It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM also has a mutase and a phosphatase function, but these are much less active, in contrast to its glycolytic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG ...

  9. Phosphoglycolate phosphatase - Wikipedia

    en.wikipedia.org/wiki/Phosphoglycolate_phosphatase

    The implication of phosphoglycolate phosphatase's role in human red blood cells was discovered when its substrate, phosphoglycolate, was shown to be a potent activator of the enzyme 2,3-bisphosphoglycerate phosphatase(2,3-DPG), another hydrolase which catalyzes the metabolic reaction of 2,3-bisphosphoglycerate to 3-phosphoglycerate. In the ...