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Interaction of organic phosphates with bovine hemoglobin

II. Oxygen binding equilibria of newborn and adult hemoglobin

  • Heart, Circulation, Respiration and Blood; Environmental and Exercise Physiology
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Abstract

We investigated oxylabile H+ binding and pH dependent oxygen binding of adult and newborn bovine hemoglobin as influenced by the organic phosphates 2,3-disphosphoglycerate (DPG), adenosine-5′-triphosphate (ATP), and myo-inositol hexaphosphate (IHP).

The oxygenaffinity of newborn bovine hemoglobin is higher than that of adult hemoglobin over a pH range of 6.5 to 8. Both DPG and IHP decrease the oxygen affinity of adult bovine hemoglobin. IHP not only decreases the oxygen affinity, but also reduces the apparent cooperativity, whereas DPG does not affect cooperativity. The rise in logP50 upon addition of DPG is about equal for adult and newborn bovine hemoglobin: at pH 7.0 we find ΔlogP50 values of 0.14 and 0.13 respectively upon addition of a fivefold excess of organic phosphate. This agrees with the identical nature of the presumed organic phosphate binding site in these two hemoglobins, but contrasts with the situation in man: newborn human hemoglobin is much less influenced by organic phosphates than adult human hemoglobin.

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Abbreviations

Hb:

(tetrameric) hemoglobin

DPG:

2,3-diphosphoglycerate

IHP:

myo-inositol hexaphosphate

Tris:

tris(hydroxymethyl)-aminomethane

bis-Tris:

bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane

ΔZH :

fixed-acid Haldane effect=amount of protons released upon full oxygenation of deoxyhemoglobin (unit: mol·mol−1)

i DPG,i IHP :

ratio between molar concentrations of DPG and Hb, and IHP and Hb, respectively (unit: mol·mol−)

P50 :

oxygen partial pressure at half oxygen saturation of Hb (unit: kPa, mm Hg)

Y:

percentile oxygen saturation of Hb

T :

absolute temperature (unit: K)

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Authors and Affiliations

  1. Department of Physiology, Faculty of Medicine, University of Nijmegen, Geert Grooteplein Noord 21A, NL-6525 EZ, Nijmegen, The Netherlands

    Peter M. Breepoel, Ferdinand Kreuzer & Marijke Hazevoet

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  1. Peter M. Breepoel
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  2. Ferdinand Kreuzer
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  3. Marijke Hazevoet
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Breepoel, P.M., Kreuzer, F. & Hazevoet, M. Interaction of organic phosphates with bovine hemoglobin. Pflugers Arch. 389, 227–235 (1981). https://doi.org/10.1007/BF00584783

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