Human whole-blood oxygen affinity: effect of carbon monoxide

1984 ◽  
Vol 57 (1) ◽  
pp. 14-20 ◽  
Author(s):  
A. Zwart ◽  
G. Kwant ◽  
B. Oeseburg ◽  
W. G. Zijlstra
Keyword(s):  
Carbon Monoxide ◽  
Whole Blood ◽  
Saturation Pressure ◽  
Oxygen Affinity ◽  
Gradual Change ◽  
Blood Oxygen ◽  
Human Whole Blood ◽  
Oxygen Dissociation ◽  
Blood Oxygen Affinity ◽  
Dissociation Curves

Oxygen dissociation curves (ODC) were recorded in the presence of carboxyhemoglobin fractions (FHbCO) up to 60%. The gradual shift to the left of the ODC at increasing amounts of HbCO was reflected in a gradual fall in the half-saturation pressure of the remaining Hb and was accompanied by a gradual change in the shape of the ODC to a hyperbolic one. The H+ factor (delta log PO2/delta pH) was determined over the entire oxygen saturation (SO2) range at three different FHbCO levels (14, 30, and 52%). At FHbCO = 14 and 30% and for the SO2 range 20–90%, the H+ factor vs. SO2 curve was not significantly different from that in the absence of HbCO. At FHbCO = 52%, however, the value found for the H+ factor (-0.55) was appreciably more negative than in the case of blood containing less than 1% HbCO (-0.44), and there was no dependence on SO2. Comparison of measured and calculated ODCs at varying HbCO fractions showed, for FHbCO less than or equal to 50%, that measured and calculated ODCs coincide over the greater part of the SO2 range. For FHbCO greater than 50%, the measured ODC was situated to the left of the calculated one over the entire SO2 range. We conclude that the heme-heme interaction for CO is appreciably larger than for O2 only for FHbCO greater than 50%, whereas for FHbCO less than 50% there is virtually no difference.

Effect of carbon monoxide on equilibrium between oxygen and hemoglobin

1976 ◽  
Vol 230 (2) ◽  
pp. 471-475 ◽  
Author(s):  
Y Okada ◽  
I Tyuma ◽  
Y Ueda ◽  
T Sugimoto
Keyword(s):  
Carbon Monoxide ◽  
Oxygen Saturation ◽  
Whole Blood ◽  
Oxygen Affinity ◽  
Hill Coefficient ◽  
Human Whole Blood ◽  
Oxygen Dissociation ◽  
Dissociation Curves ◽  
The Hill ◽  
Good Agreement

Oxygen dissociation curves of partially CO-saturated human whole blood drawn freshly or preserved more than 3 wk were studied. With increasing CO-hemoglobin concentrations, oxygen affinity of the blood increased and the Hill coefficient, n, fell and gradually approached unity. The changes induced by CO-hemoglobin showed practically no difference in the presence or absence of 2,3-diphosphoglycerate. The Bohr coefficient, deltalog P50/deltapH, was determined as a function of oxygen saturation for various concentrations of CO-hemoglobin. The coefficient remained essentially unchanged in the presence of CO-hemoglobin. In the presence of less than 50% CO-hemoglobin, a good agreement was observed between the observed oxygen dissociation curves and the curves calculated according to Roughton and Darling (Am. J. Physiol. 141: 17-31, 1944). Based on these results, physiological implications of carboxyhemoglobinemia are discussed quantitatively in comparison with methemoglobinemia.

Increased blood oxygen affinity during digestion in the snakePython molurus

2002 ◽  
Vol 205 (21) ◽  
pp. 3327-3334 ◽  
Author(s):  
Johannes Overgaard ◽  
Tobias Wang
Keyword(s):  
Partial Pressure ◽  
Oxygen Transport ◽  
Oxygen Affinity ◽  
Arterial Oxygen ◽  
Blood Oxygen ◽  
Arterial Blood ◽  
Oxygen Dissociation ◽  
Blood Oxygen Affinity ◽  
Dissociation Curves

SUMMARYMany snakes exhibit large increases in metabolic rate during digestion that place extensive demands on efficient oxygen transport. In the present study,we describe blood oxygen affinity following three weeks of fasting and 48 h after feeding in the Burmese python (Python molurus). We also report simultaneous measurements of arterial blood gases and haematological parameters. Arterial blood was obtained from chronically implanted catheters,and blood oxygen-dissociation curves were constructed from oxygencontent measurements at known oxygen partial pressure(PO2) values at 2% and 5% CO2. Arterial pH remained constant at approximately 7.6 after feeding, but digestion was associated with an approximately 6 mmol l-1 increase in [HCO3-], while CO2 partial pressure(PCO2) increased from 2.21±0.13 kPa in fasted animals to 2.89±0.17 kPa at 48 h after feeding. Blood oxygen affinity in vivo was predicted on the basis of pH in vivoand the blood oxygen-dissociation curves obtained in vitro. The blood oxygen affinity in vivo increased during digestion, with P50 values decreasing from 4.58±0.11 kPa to 3.53±0.24 kPa. This increase was associated with a significant decrease in the red blood cell [NTP]/[Hb4] ratio (relationship between the concentrations of organic phosphates and total haemoglobin) and a significant decrease in mean cellular haemoglobin content, which is indicative of swelling of the red blood cells. Our data for blood oxygen affinity and arterial oxygen levels, together with previously published values of oxygen uptake and blood flows, allow for a quantitative evaluation of oxygen transport during digestion. This analysis shows that a large part of the increased metabolism during digestion is supported by an increased venous extraction, while arterial PO2(PaO2) and haemoglobin saturation do not vary with digestive status. Thus, we predict that venous PO2 (PvO2) is reduced from a fasting value of 5.2 kPa to 1.6 kPa during digestion.

Postnatal regulation of canine oxygen delivery: erythrocyte components affecting Hb function

1980 ◽  
Vol 238 (1) ◽  
pp. H73-H79 ◽  
Author(s):  
P. A. Mueggler ◽  
G. Jones ◽  
J. S. Peterson ◽  
J. M. Bissonnette ◽  
R. D. Koler ◽  
...  
Keyword(s):  
Oxygen Affinity ◽  
Fetal Hemoglobin ◽  
Blood Oxygen ◽  
Oxygen Dissociation ◽  
Affinity Change ◽  
Blood Oxygen Affinity ◽  
Postnatal Change ◽  
2,3 Dpg

A rightward shift in the blood oxygen dissociation curve occurs during the 1st mo of canine life. A detailed peptide analysis indicated that dogs do not have a separate fetal hemoglobin. Other erythrocyte components such as ATP, K+, Na+, and H+ were excluded as significant mediators of the postnatal oxygen affinity change. Erythrocyte 2,3-DPG levels essentially zero in fetal dogs, increased rapidly during the 1st mo of canine life. There was a significant correlation between this postnatal 2,3-DPG increase and the postnatal decrease in blood oxygen affinity. Dialyzed hemolysates of fetal or adult canine blood have the same intrinsic oxygen affinity and the same response to normal adult levels of 2,3-DPG. Furthermore, the magnitude and direction of this 2,3-DPG-induced decrease in oxygen affinity in vitro are comparable to the in vivo postnatal change in oxygen affinity.

scholarly journals Oxygen Affinity in Hemoglobin Köln Disease

Blood ◽  
1972 ◽  
Vol 39 (3) ◽  
pp. 398-406 ◽  
Author(s):  
Frank G. de Furia ◽  
Denis R. Miller
Keyword(s):  
Whole Blood ◽  
Normal Values ◽  
Cell Mass ◽  
Oxygen Affinity ◽  
Red Cell ◽  
Blood Oxygen ◽  
Red Cell Mass ◽  
High Oxygen Affinity ◽  
Blood Oxygen Affinity

Abstract Oxygen affinity studies in a splenectomized patient with sporadically occurring Hb Köln disease revealed high whole blood oxygen affinity (P50 O2 17.6 mm Hg) with increased 2, 3-diphosphoglycerate (DPG), low ATP, and normal RBC ΔpH. Isolated electrophoretically slow migrating Hb Köln had a high oxygen affinity, decreased Hill’s number, and normal DPG reactivity. Functional evidence for hybrid tetramers with normal mobility is presented. Partial deoxygenation may play a role in the denaturation of the Hb Köln molecule and thus account for a higher oxygen affinity (low P50 O2), measured by the mixing technique, than the actual values for P50 that exist in vivo. Increased oxygen affinity and decreased P50 O2 would result in increased erythropoiesis and account for a well-compensated hemolytic process in this patient with a normal red cell mass and normal values of hemoglobin.

Effect of Metrizamide on Whole Blood Oxygen Affinity

1978 ◽  
Vol 19 (4) ◽  
pp. 688-692 ◽  
Author(s):  
S. Berglund ◽  
T. Almén ◽  
B. W. Johansson
Keyword(s):  
Whole Blood ◽  
Oxygen Affinity ◽  
Blood Oxygen ◽  
Blood Oxygen Affinity

scholarly journals Oxygenational properties and phosphorylated metabolic intermediates in blood and erythrocytes of the dogfish, Squalus acanthias

1983 ◽  
Vol 103 (1) ◽  
pp. 95-108
Author(s):  
R. M. Wells ◽  
R. E. Weber
Keyword(s):  
Thin Layer ◽  
Whole Blood ◽  
Oxygen Affinity ◽  
Squalus Acanthias ◽  
Blood Oxygen ◽  
Equilibrium Curve ◽  
Metabolic Intermediates ◽  
Blood Oxygen Affinity ◽  
Layer Chromatography ◽  
Haldane Effect

A typical whole blood O2-equilibrium curve from Squalus acanthias had a P50 of 13.2 mmHg and was slightly sigmoidal, having an n value of 1.6 at 15 degrees C, PCO2 = 2.2 mmHg (pH = 7.85). A small Bohr effect was present (phi = −0.28) together with a weak Haldane effect and no Root shift. The predominant trinucleotide, determined by thin layer chromatography, was ATP (0.44 +/− 0.13 S.D. mmol 1(−1) blood) with smaller amounts of GTP present (0.07 +/− 0.02) S.D. mmol 1(−1). Total nucleotide concentrations, determined enzymatically, were low by comparison with teleosts. Incubation of erythrocytes with or without oxygen, or in the presence of a metabolite-enriched ‘cocktail’ showed limited potential for phosphate cofactor regulation of blood oxygen affinity.

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