Any synthetic analogue of Hemoglobin or any other Xenobiological agents can be cited as example. Please provide links and references.
Myo-inositol trispyrophospate (ITPP) shifts the oxyhemoglobin dissociation curve to the right, thus decreases hemoglobin affinity for oxygen and results in an increased oxygen delivery to the tissue. I has been considerd as a potential agent used in dopping of athlete and a performance-enhancing substance in horse racing.
Biolo, A; Greferath, R; Siwik, DA; Qin, F; Valsky, E; Fylaktakidou, KC; Pothukanuri, S; Duarte, CD; Schwarz, RP; Lehn, JM; Nicolau, C; Colucci, WS (2009). "Enhanced exercise capacity in mice with severe heart failure treated with an allosteric effector of hemoglobin, myo-inositol trispyrophosphate". Proc Natl Acad Sci U S A. 106 (6): 1926–1929.
Lam, G; Zhao, S; Sandhu, J; Yi, R; Loganathan, D; Morrissey, B (2014). "Detection of myo-inositol tris pyrophosphate (ITPP) in equine following an administration of ITPP". Drug Test. Anal. 6 (3): 268–276
Myo-inositol trispyrophospate (ITPP) shifts the oxyhemoglobin dissociation curve to the right, thus decreases hemoglobin affinity for oxygen and results in an increased oxygen delivery to the tissue. I has been considerd as a potential agent used in dopping of athlete and a performance-enhancing substance in horse racing.
Biolo, A; Greferath, R; Siwik, DA; Qin, F; Valsky, E; Fylaktakidou, KC; Pothukanuri, S; Duarte, CD; Schwarz, RP; Lehn, JM; Nicolau, C; Colucci, WS (2009). "Enhanced exercise capacity in mice with severe heart failure treated with an allosteric effector of hemoglobin, myo-inositol trispyrophosphate". Proc Natl Acad Sci U S A. 106 (6): 1926–1929.
Lam, G; Zhao, S; Sandhu, J; Yi, R; Loganathan, D; Morrissey, B (2014). "Detection of myo-inositol tris pyrophosphate (ITPP) in equine following an administration of ITPP". Drug Test. Anal. 6 (3): 268–276
Cooperativity enhances oxygen delivery by hemoglobin. Because of coopertivity between O2 - binding sites, hemoglobin delivers more O2 to tissues than would a noncooperative protein (pO2, partial pressure of oxygen). Several molecules are responsible for substantially lowering lowering hemoglobin's ability to transport oxygen to tissues. The most common is carbon monoxide ( CO ), which has a binding affinity to hemoglobin 200 times greater than oxygen. For more details consult https://www.ncbi.nlm.nih.gov --books
Indeed, as very correctly stated by Sylvester, CO prevents O2 binding to hemoglobin and thus transport of O2 from the lung to the tissues. Thus CO is the opposite of a compound that would make "Hemoglobin ... potentially carry more oxygen to bloodstream" (Sumit's question). CO poisoning is a life threatening condition too often leading to death.
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