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  2. 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.

  3. 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 ...

  4. Bisphosphoglycerate mutase - Wikipedia

    en.wikipedia.org/wiki/Bisphosphoglycerate_mutase

    Because the main function of bisphosphoglycerate mutase is the synthesis of 2,3-BPG, this enzyme is found only in erythrocytes and placental cells. [2] In glycolysis, converting 1,3-BPG to 2,3-BPG would be very inefficient, as it just adds another unnecessary step. Since the main role of 2,3-BPG is to shift the equilibrium of hemoglobin toward ...

  5. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    At the placenta, there is a higher concentration of 2,3-BPG formed, and 2,3-BPG binds readily to beta chains rather than to alpha chains. As a result, 2,3-BPG binds more strongly to adult hemoglobin, causing HbA to release more oxygen for uptake by the fetus, whose HbF is unaffected by the 2,3-BPG. [10]

  6. 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.

  7. Food poisoning is extremely common. But that doesn't ... - AOL

    www.aol.com/food-poisoning-extremely-common...

    Few things will put a damper on your vacation or holiday faster than food poisoning. The intense stomach pain, rushing to the toilet and feeling relegated to bed keeps just about everyone out of ...

  8. 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 ...

  9. UNITED STATES DISTRICT COURT FOR THE DISTRICT OF COLUMBIA

    images.huffingtonpost.com/2013-03-09-amicus.pdf

    organized under Section 501(c)(3) of the Internal Revenue Code and under New York State law, without any parent corporation, that it has issued no stock, and that there thus is no publicly held company that owns any such stock. Case 1:10-cv-01067-RBW-DAR Document 212 Filed 12/14/12 Page 2 of 38