On the respiratory function of haemoglobin

Bauer, Christian

doi:10.1007/bfb0034292

Cited by 54 publications

(7 citation statements)

References 169 publications

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“…BAYER [7] calculated that in this case the arterio-mixed venous difference in oxygen saturation will be 75 . If there is no classical Bohr effect and the pH remains 7.414, the arterio-mixed venous difference will be 62 %.…”

Section: Molecular Mechanism Of the Bohr Effectmentioning

confidence: 98%

“…Under normal physiological conditions, however, changes in the DPG activity seem to be unimportant as long as the total DPG concentration is constant [18]. The classical Haldane coefficient can be defined as the change in total carbon dioxide per heme, [C02], due to the change in oxygen saturation at constant Pc0 2, and expressed as follows [ [7,29]. Evidently, the classical Bohr and Haldane effects are not equivalent.…”

Section: Thermodynamical Relation Between the Bohr Effect And The Halmentioning

confidence: 99%

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The Bohr effect and the Haldane effect in human hemoglobin.

Tyuma

1984

Jpn.J.Physiol

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In 1904, BOHR, HASSEL$ALCH, and KROGH [11] discovered that increased carbon dioxide pressure (Pcoz) shifts the oxygen equilibrium curve of blood to the right, i.e., the oxygen affinity of blood is inversely proportional to Pcoz. There was much discussion at that time as to whether the shift due to C02 could be explained entirely by the concomitant change in pH, or whether C02 has, in addition, a specific effect. It has now been shown that C02 does exert a specific effect due to its direct combination with hemoglobin to form carbamino compound [27]. Thus, the original observation of Bohr et al., now called "classical Bohr effect" [19,39], is a composite of the specific effects of C02 and Ht The separate effect of pH on the oxygen affinity of hemoglobin has conventionally been referred to as the Bohr effect : between pH 6 and 9 the fall of pH decreases the oxygen affinity (the alkaline Bohr effect) and below pH 6 the oxygen affinity rises with falling pH (the acid or reverse Bohr effect).On the other hand, the reduction of C02 content in blood on oxygenation at constant Pcoz was demonstrated by CHISTIANSEN, DOUGLAS, and HALDANE [13] in 1914. This "classical Haldane effect" [39] is a thermodynamic corollary of the classical Bohr effect and can be explained by the decrease in carbamino binding to hemoglobin and the fall in pH on oxygenation. The release and uptake of protons on oxygenation and deoxygenation of hemoglobin are now defined as the Haldane effect. Sometimes both the Bohr and Haldane effects, including the classical ones, are collectively termed the Bohr effect.It is now well-established that in addition to protons and carbon dioxide, 2, 3-diphosphoglycerate (DPG), the major organic phosphate in mammalian erythrocytes, tremendously decreases the oxygen affinity of hemoglobin by binding to the deoxy form of the protein preferentially [9]. Other salt anions, e.g., chloride and inorganic phosphate, also show a similar but lesser effect [24]. Although the binding sites of these ligands are remote from the heme iron atom, the bindings are related to the oxygenation of the iron atom and have been described as "oxygen-linked" or "oxylabile." The interactions between the oxygen-binding sites and the sites for the non-heme ligands are referred to as the heterotropic allosteric

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Section: Molecular Mechanism Of the Bohr Effectmentioning

confidence: 98%

Section: Thermodynamical Relation Between the Bohr Effect And The Halmentioning

confidence: 99%

The Bohr effect and the Haldane effect in human hemoglobin.

Tyuma

1984

Jpn.J.Physiol

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“…Competition between 2,3-P2 -glycerate and CO2 for the binding sites of human deoxyhemoglobin tetramer have been demonstrated (Bauer 1974) and the binding of inositol hexakisphosphate (inositol-P6 ) to human de oxyhemoglobin is similar to that of 2,3-P2 -glycerate (Arnone and Perutz 1974). Further studies indicated a similar competition between inositol-P6 and CO2 for binding sites in human deoxyhemoglobin and implied a similar reaction forinositol-Ps and CO2 in chicken hemoglobin (Benesch et al 1968;Wells 1976).…”

Section: Discussionmentioning

confidence: 85%

The Relationship Between Erythrocyte Phosphate Metabolism, Carbon Dioxide, and pH on Blood Oxygen Affinity in Birds

Isaacks

1985

Proceedings in Life Sciences

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“…A decrease in oxygen affinity (high P50 value) of blood enhances the release of oxygen from haemoglobin to the tissues [9] and compensates for the decreased cardiac output and/or reduced oxygen content of blood [4]. The accepted assumption that a high P50 value implies an increased oxygen unloading capacity of blood is not applicable at low arterial tensions [8], i.e., on the steep part of the oxygen dissociation curve.…”

Section: Discussionmentioning

confidence: 99%

Fetal oxygen affinity and its parameters in a random obstetric population

Rg¹

1983

Journal of Perinatal Medicine

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On the respiratory function of haemoglobin

Cited by 54 publications

References 169 publications

The Bohr effect and the Haldane effect in human hemoglobin.

The Bohr effect and the Haldane effect in human hemoglobin.

The Relationship Between Erythrocyte Phosphate Metabolism, Carbon Dioxide, and pH on Blood Oxygen Affinity in Birds

Fetal oxygen affinity and its parameters in a random obstetric population

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