Oxygen affinity of hemoglobin in postmenopausal women

Humpeler, Egon; Vogel, Sylvia; Ladner, Maria; Pohl, Peter

doi:10.1007/bf01063866

Cited by 2 publications

(1 citation statement)

References 6 publications

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“…The Bohr effect, which in the physiological pH range causes an increase of PO 2 at constant saturation by acidification (essential in working muscles), may vary depending on various factors like oxygen saturation [27], [28], type of acid [27], [28], substance concentrations and age of the erythrocytes (e. g. [29]); in altitude residents a tendency to lowered Bohr coefficients (BC = ΔlogPO 2 /ΔpH) has been observed [30], [31]. Also sex differences in oxygen binding properties have been described: women [32]–[34] as well as children [35] tend to higher P 50 st than men. Finally in vivo variations of the ODC in venous blood of anemic patients as well as of trained subjects have been observed during exercise which were no more detectable after in vitro equilibration of blood [36]–[38].…”

Section: Introductionmentioning

confidence: 99%

Hemoglobin Oxygen Affinity in Patients with Cystic Fibrosis

et al. 2014

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In patients with cystic fibrosis lung damages cause arterial hypoxia. As a typical compensatory reaction one might expect changes in oxygen affinity of hemoglobin. Therefore position (standard half saturation pressure P50st) and slope (Hill’s n) of the O2 dissociation curve as well as the Bohr coefficients (BC) for CO2 and lactic acid were determined in blood of 14 adult patients (8 males, 6 females) and 14 healthy controls (6 males, 8 females). While Hill’s n amounted to approximately 2.6 in all subjects, P50st was slightly increased by 1mmHg in both patient groups (controls male 26.7±0.2, controls female 27.0±0.1, patients male 27.7±0.5, patients female 28.0±0.3 mmHg; mean and standard error, overall p<0.01). Main cause was a rise of 1–2 µmol/g hemoglobin in erythrocytic 2,3-biphosphoglycerate concentration. One patient only, clearly identified as an outlier and with the mutation G551D, showed a reduction of both P50st (24.5 mmHg) and [2,3-biphosphoglycerate] (9.8 µmol/g hemoglobin). There were no differences in BCCO2, but small sex differences in the BC for lactic acid in the controls which were not detectable in the patients. Causes for the right shift of the O2 dissociation curve might be hypoxic stimulation of erythrocytic glycolysis and an increased red cell turnover both causing increased [2,3-biphosphoglycerate]. However, for situations with additional hypercapnia as observed in exercising patients a left shift seems to be a more favourable adaptation in cystic fibrosis. Additionally when in vivo PO2 values were corrected to the standard conditions they mostly lay left of the in vitro O2 dissociation curve in both patients and controls. This hints to unknown fugitive factors influencing oxygen affinity.

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Section: Introductionmentioning

confidence: 99%

Hemoglobin Oxygen Affinity in Patients with Cystic Fibrosis

et al. 2014

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Oxygen Transport by Hemoglobin

Mairbäurl

Weber

2012

Comprehensive Physiology

169

161

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Hemoglobin (Hb) constitutes a vital link between ambient O 2 availability and aerobic metabolism by transporting oxygen (O 2 ) from the respiratory surfaces of the lungs or gills to the O 2 ‐consuming tissues. The amount of O 2 available to tissues depends on the blood‐perfusion rate, as well as the arterio‐venous difference in blood O 2 contents, which is determined by the respective loading and unloading O 2 tensions and Hb‐O 2 ‐affinity. S hort‐term adjustments in tissue oxygen delivery in response to decreased O 2 supply or increased O 2 demand (under exercise, hypoxia at high altitude, cardiovascular disease, and ischemia) are mediated by metabolically induced changes in the red cell levels of allosteric effectors such as protons (H + ), carbon dioxide (CO 2 ), organic phosphates, and chloride (Cl − ) that modulate Hb‐O 2 affinity. The long‐term , genetically coded adaptations in oxygen transport encountered in animals that permanently are subjected to low environmental O 2 tensions commonly result from changes in the molecular structure of Hb, notably amino acid exchanges that alter Hb's intrinsic O 2 affinity or its sensitivity to allosteric effectors. Structure‐function studies of animal Hbs and human Hb mutants illustrate the different strategies for adjusting Hb‐O 2 affinity and optimizing tissue oxygen supply. © 2012 American Physiological Society. Compr Physiol 2:1463‐1489, 2012.

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Oxygen affinity of hemoglobin in postmenopausal women

Cited by 2 publications

References 6 publications

Hemoglobin Oxygen Affinity in Patients with Cystic Fibrosis

Hemoglobin Oxygen Affinity in Patients with Cystic Fibrosis

Oxygen Transport by Hemoglobin

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