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The Influence of MgCl2 on the O2-Hb-Binding Curve of Human Hemoglobin Under Intracellular Conditions

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 75))

Abstract

In 1969 a model was proposed (BARNIKOL et al.) to explain the effect of the Hb- concentration on the O2- Hb- binding curve (GROTE, 1967). The existence of at least one low molecular substance (called Z) besides H and CO2 was postulated, which is equimolar with Hb (≈ 5 mM) and which is bound preferentially to deoxy- Hb. From a simple stoichiometric consideration it follows, that a substance can only have a measurable influence on the O2- Hb- binding curve, if its molar concentration is not to low compared with the molar Hb- concentration. For example, 2,3- diphosphogly-cerate (= DPG), glutathione and Mg++ have intracellular concentrations of the necessary magnitude. Only a small part of Magnesium is bound to the membrane of the erythrocytes (HARRISON et al.). Principally all these substances are candidates for Z. In 1967 it was shown by BENESCH et al. and by CHANUTIN et al., that ATP and DPG influence the O2-Hb- binding curve as was postulated for Z, and it was shown (BENESCH et al., 1968), that the organic phosphates are bound preferentially to deoxy-Hb. In our speculation on the chemical nature of Z first we prefered Mg++ because of its complex forming properties. It is known for a long time, that Mg++ forms a complex with ATP (MARTELL et al.,1956) and in 1970 it was found, that DPG forms also a complex with Mg++ (COLLIER et al.).

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Literature

  • G. Amiconi, E. Antonini, M. Brunori, J. Wyman in “Hemoglobin and Myoglobin in thin Reactions with ligands”, authors: E. Antonini and M. Brunori, North- Holland Publishing Company, Amsterdam — London, 1971, p.246

    Google Scholar 

  • W.K.R. Barnikol, G. Thews Zur Interpretation der O2- Bindungskurve des Human- Hämoglobins. Pflügers Arch. 309, 232–249 (1969)

    Article  PubMed  CAS  Google Scholar 

  • W.K.R. Barnikol, W. Wahler On the Accuracy of an Improved Method for the Measurement of O2- Dissociation Curves According to NIESEL and THEWS, 1961. Adv. in Exp. Medicine and Biology 37A, 325–331 (1973) (Editors: D.F. Bruley, H.I. Bicher), Plenum Press, New York- London

    CAS  Google Scholar 

  • R. Benesch, R.E. Benesch The Effect of Organic Phosphates from the Human Erythrocyte on the Allosteric Properties of Hemoglobin. Biochem. Biophys. Res. Comm. 26, 162–167 (1967)

    Article  PubMed  CAS  Google Scholar 

  • R. Benesch, R.E. Benesch, C.I. Yu Reciprocal Binding of Oxygen and Diphosphoglycerate by Human Hemoglobin. Proc. Nat. Acad. Sci. (Wash.) 59, 526–532 (1968)

    Article  CAS  Google Scholar 

  • H. Berger, G.R. Jänig, G. Gerber, K. Ruckpaul, S.M. Rapoport Interaction of Hemoglobin with Ions. Interactions among Magnesium, Adenosine 5- Triphosphate, 2,3- Biphosphoglycerate, and Oxygenated and Deoxygenated Human Hemoglobin under Simulated Intracellular Conditions. Eur. J. Biochem. 38, 553–562 (1973)

    Article  PubMed  CAS  Google Scholar 

  • H.F. Bunn, B.J. Ransil, A. Chao The Interaction between Erythrocyte Organic Phosphates, Magnesium Ion, and Hemoglobin. J. Biol Chem. 246, 5273–5279 (1971)

    PubMed  CAS  Google Scholar 

  • A. Chanutin, R. Curnish Effect of Organic and Inorganic Phosphates on the Oxygen Equilibrium of Human Erythrocytes. Arch. Biochem. 121, 96–102 (1967)

    Article  PubMed  CAS  Google Scholar 

  • H.B. Collier A. Lam Binding of Ca2+ and Mg2+ by 2,3 Diphosphoglycerate. Biochim. Biophys. Acta 222, 299–306 (1970)

    Article  PubMed  CAS  Google Scholar 

  • L. Garby, G. Gerber, C.H. de Verdier Binding of 2,3 — Diphosphoglycerate and Adenosine Triphosphate to Human Hemoglobin A. Eur. J. Biochem. 10, 110–115 (1969)

    Article  PubMed  CAS  Google Scholar 

  • L. Garby, C.H. de Verdier Affinity of Human Hemoglobin to 2,3- Diphosphoglycerate. Effect of Hemoglobin Concentration and pH. Scand. J. Clin. Lab. Invest. 27, 345–350 (1971)

    Article  PubMed  CAS  Google Scholar 

  • J. Grote Die Bestimmung der Sauerstoff- Bindungskurve von hochverdünnten Hämoglobinlösungen. Pflügers Arch. 296, 202–211 (1967)

    Article  CAS  Google Scholar 

  • D.G. Harrison, C. Long The Calcium Content of Human Erythrocytes. J. Physiol. 199, 367–381 (1968)

    PubMed  CAS  Google Scholar 

  • A.E. Martel I, G. Schwarzenbach Adenosinphosphate und Triphosphat als Komplexbildner für Calcium und Magnesium. Helv. Chim. Acta 39, 653–661 (1956)

    Article  Google Scholar 

  • J.R. Murphy The Influence of pH on Physical Properties of the Erythrocyte. in “Stoffwechsel- und Membranpermeabilitäten von Erythrocyten und Thrombocyten”, Thieme, Stuttgart 1968, p. 452

    Google Scholar 

  • O. Siggaard- Andersen Oxygen- Linked Hydrogen Ion Binding of Human Hemoglobin. Effects of Carbon- Dioxide and 2,3- Diphosphoglycerate. I. Studies on Erythrolysate. Scand. J. Clin. Lab. Invest. 27, 351–360 (1971)

    Article  Google Scholar 

  • O. Warburg, W. Christian Isolierung und Kristallisation des Gärungsfermentes Enolase. Biochem. Zeitschr. 310, 384–425 (1942)

    CAS  Google Scholar 

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© 1976 Plenum Press, New York

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Barnikol, W. (1976). The Influence of MgCl2 on the O2-Hb-Binding Curve of Human Hemoglobin Under Intracellular Conditions. In: Grote, J., Reneau, D., Thews, G. (eds) Oxygen Transport to Tissue — II. Advances in Experimental Medicine and Biology, vol 75. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3273-2_13

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  • DOI: https://doi.org/10.1007/978-1-4684-3273-2_13

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3275-6

  • Online ISBN: 978-1-4684-3273-2

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