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Effect of RSR13 on Temperature-Dependent Changes in Hemoglobin Oxygen Affinity of Human Whole Blood

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Oxygen Transport to Tissue XX

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 454))

Abstract

RSR13, 2-[4-[[(3,5-Dimethylanilino)carbonyl]methyl]phenoxy]-2-methylpropionic acid sodium salt (MW 363), is a synthetic allosteric modifier of hemoglobin (Figure 1). RSR13 is a small molecule that noncovalently binds in the central water cavity of the hemoglobin tetramer, reduces hemoglobin-oxygen (Hb-O2) affinity1 and enhances the diffusion of oxygen from the blood to the tissues.2,3,4 RSR13 emulates the function of natural allosteric modifiers such as hydrogen ions, carbon dioxide, and 2,3-diphosphoglycerate. This therapeutic strategy of “turbocharging” oxygen unloading from hemoglobin to tissue emulates and amplifies physiological tissue oxygenation. This approach has potential application in clinical conditions characterized by tissue hypoxia due to: 1) inadequate blood flow (regional or global), 2) insufficient oxygen carrying capacity (e.g., hemorrhage or dilutional anemia), 3) increased tissue oxygen demand unmatched by supply, and/or 4) insufficient oxygen loading/unloading capacity of hemoglobin (e.g., hypothermia).

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Steffen, R.P. (1998). Effect of RSR13 on Temperature-Dependent Changes in Hemoglobin Oxygen Affinity of Human Whole Blood. In: Hudetz, A.G., Bruley, D.F. (eds) Oxygen Transport to Tissue XX. Advances in Experimental Medicine and Biology, vol 454. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4863-8_77

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  • DOI: https://doi.org/10.1007/978-1-4615-4863-8_77

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7206-6

  • Online ISBN: 978-1-4615-4863-8

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