Influence of carbon monoxide on hemoglobin-oxygen binding

1976 ◽  
Vol 41 (6) ◽  
pp. 893-899 ◽  
Author(s):  
M. P. Hlastala ◽  
H. P. McKenna ◽  
R. L. Franada ◽  
J. C. Detter
Keyword(s):  
Carbon Monoxide ◽  
Oxygen Affinity ◽  
Co2 Concentration ◽  
Bohr Effect ◽  
Oxygen Binding ◽  
Dissociation Curve ◽  
Low Oxygen ◽  
Oxygen Dissociation ◽  
Initial Binding ◽  
Fixed Acid

The oxygen dissociation curve and Bohr effect were measured in normal whole blood as a function of carboxyhemoglobin concentration [HbCO]. pH was changed by varying CO2 concentration (CO2 Bohr effect) or by addition of isotonic NaOH or HCl at constant PCO2 (fixed acid Bohr effect). As [HbCO] varied through the range of 2, 25, 50, and 75%, P50 was 26.3, 18.0, 11.6, and 6.5 mmHg, respectively. CO2 Bohr effect was highest at low oxygen saturations. This effect did not change as [HbCO] was increased. However, as [HbCO] was increased from 2 to 75%, the fixed acid Bohr factor increased in magnitude from -0.20 to -0.80 at very low oxygen saturations. The effect of molecular CO2 binding (carbamino) on oxygen affinity was eliminated at high [HbCO]. These results are consistent with the initial binding of O2 or CO to thealpha-chain of hemoglobin. The results also suggest that heme-heme interaction is different for oxygen than for carbon monoxide.

The Bohr effect related to blood and erythrocyte pH

1963 ◽  
Vol 205 (2) ◽  
pp. 337-340 ◽  
Author(s):  
Peter Hilpert ◽  
Renate Gislinde Fleischmann ◽  
Doris Kempe ◽  
Heinz Bartels
Keyword(s):  
Oxygen Pressure ◽  
Ph Value ◽  
Oxygen Affinity ◽  
Bohr Effect ◽  
Red Cell ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
Oxygen Dissociation ◽  
Constant Cell ◽  
The Right

The Bohr effect of the blood and the red cell hemolysates of adult and newborn humans, goats and kids, and sheep and lambs were determined and the physiological significance is discussed. Similar determinations were made on blood from an African elephant, yak, camel, Dybowski deer, and llama. The strong displacement to the right of the oxygen dissociation curve which occurs in kids and lambs during the first 5 days of life can be largely explained by a change in the pH value within the erythrocytes. When the oxygen affinity is expressed by the oxygen pressure necessary for half saturation (T50) at a constant cell pH, considerable differences exist between species.

Saturation dependency of the Bohr effect: interactions among H-+, CO2, and DPG

1975 ◽  
Vol 38 (6) ◽  
pp. 1126-1131 ◽  
Author(s):  
M. P. Hlastala ◽  
R. D. Woodson
Keyword(s):  
Oxygen Saturation ◽  
Base Excess ◽  
Oxygen Affinity ◽  
Co2 Concentration ◽  
Bohr Effect ◽  
Blood Oxygen Saturation ◽  
Relative Contribution ◽  
Lower Oxygen ◽  
Lower Saturation ◽  
Fixed Acid

The Bohr effect was measured in normal whole blood and in blood with low DPG concentration as a function of oxygen saturation. pH was changed by varying CO2 concentration (CO2 Bohr effect) or by addition of isotonic NaOH or HC1 at constant PCO2 (fixed acid Bohr effect). At nornal DPG concentration CO2 Bohr effect was -0.52 at 50% blood oxygen saturation, increasing in magnitude at lower saturation and decreasing in magnitude at higher saturation. In DPG depleted blood with base excess (BE) similar to 0 meq/1, there was similar dependence of CO2 Bohr effect on oxygen saturation. At BE similar to -10 meq/1, influence of saturation was comparable, but the magnitude of the Bohr effect was markedly increased at all saturations. Fixed acid Bohr effect at normal DPG concentration was -0.45 at saturations of 50–90% but decreased at lower saturations. In DPG-depleted blood fixed acid Bohr effect averaged about -0.33 with minimal variation with saturation. Influence of DPG on oxygen affinity was greater at intermediate saturations and less at saturations below 20% and above 80%. Effect of CO2, independent of pH, was many fold greater at lower oxygen saturations than at higher saturations. These results support the suggestion that the alpha chain of hemoglobin is the site of the initial oxygenation reaction. Physiologically they indicate that the relative contribution of CO2 and fixed acid, as well as the level of oxygen saturation and DPG concentration, may be important in determining PO2 of capillary blood and resulting oxygen delivery.

Chloride and inorganic phosphate modulate binding of oxygen to bovine red blood cells

1994 ◽  
Vol 77 (1) ◽  
pp. 202-208 ◽  
Author(s):  
P. Gustin ◽  
B. Detry ◽  
M. L. Cao ◽  
F. Chenut ◽  
A. Robert ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Oxygen Affinity ◽  
Oxygen Binding ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
Oxygen Dissociation ◽  
Hemoglobin Saturation ◽  
The Difference ◽  
The Right

The influence of Pi and Cl on the equilibrium of oxygen binding to bovine red blood cells was assessed by plotting the whole blood oxygen dissociation curve measured under standard conditions with and without added KCl and K2HPO4. Both salts shifted the oxygen dissociation curve to the right. This effect was more marked at the highest saturation levels. At a given saturation level, the anion-induced shift was linearly related to the concentration of salt added to the blood. Cl had a greater effect than Pi. The relationship between changes in Po2 at 50% hemoglobin saturation (in Torr) and concentrations of ions added (in mmol/l) was equal to 0.0515[Cl] + 0.0302[Pi] (r2 = 0.94; P < 0.001). These changes were not due to the hyperosmolality induced by salt addition, since sucrose added in place of salts was without effect on the measured parameters. The oxygen exchange fraction expressed as percentage of saturation, i.e., the difference in hemoglobin saturation when Po2 decreases from 130 to 40 Torr, was linearly correlated to added anion concentration (in mmol/l) (= 0.102[Cl] + 0.059[Pi] (r2 = 0.95; P < 0.001)). No significant interaction between the anions was observed; their effects were purely additive. This original mechanism of controlling the oxygen affinity of bovine blood may have clinical relevance: Cl and Pi could be used to increase oxygen transport efficiency in hypoxic animals.

scholarly journals Haemoglobin polymorphisms affect the oxygen-binding properties in Atlantic cod populations

2008 ◽  
Vol 276 (1658) ◽  
pp. 833-841 ◽  
Author(s):  
Øivind Andersen ◽  
Ola Frang Wetten ◽  
Maria Cristina De Rosa ◽  
Carl Andre ◽  
Cristiana Carelli Alinovi ◽  
...  
Keyword(s):  
Evolutionary Biology ◽  
Quaternary Structure ◽  
Atlantic Cod ◽  
Three Dimensional ◽  
Oxygen Affinity ◽  
Oxygen Binding ◽  
Low Oxygen ◽  
Binding Properties ◽  
Important Species ◽  
The North

A major challenge in evolutionary biology is to identify the genes underlying adaptation. The oxygen-transporting haemoglobins directly link external conditions with metabolic needs and therefore represent a unique system for studying environmental effects on molecular evolution. We have discovered two haemoglobin polymorphisms in Atlantic cod populations inhabiting varying temperature and oxygen regimes in the North Atlantic. Three-dimensional modelling of the tetrameric haemoglobin structure demonstrated that the two amino acid replacements Met55β 1 Val and Lys62β 1 Ala are located at crucial positions of the α 1 β 1 subunit interface and haem pocket, respectively. The replacements are proposed to affect the oxygen-binding properties by modifying the haemoglobin quaternary structure and electrostatic feature. Intriguingly, the same molecular mechanism for facilitating oxygen binding is found in avian species adapted to high altitudes, illustrating convergent evolution in water- and air-breathing vertebrates to reduction in environmental oxygen availability. Cod populations inhabiting the cold Arctic waters and the low-oxygen Baltic Sea seem well adapted to these conditions by possessing the high oxygen affinity Val55–Ala62 haplotype, while the temperature-insensitive Met55–Lys62 haplotype predominates in the southern populations. The distinct distributions of the functionally different haemoglobin variants indicate that the present biogeography of this ecologically and economically important species might be seriously affected by global warming.

scholarly journals Hemoglobin Non-equilibrium Oxygen Dissociation Curve

2020 ◽  
Author(s):  
Rosella Scrima ◽  
Sabino Fugetto ◽  
Nazzareno Capitanio ◽  
Domenico L. Gatti
Keyword(s):  
Partial Pressure ◽  
Correct Diagnosis ◽  
Oxygen Affinity ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
High Affinity ◽  
Oxygen Dissociation ◽  
Sequential Binding ◽  
Non Equilibrium

AbstractAbnormal hemoglobins can have major consequences for tissue delivery of oxygen. Correct diagnosis of hemoglobinopathies with altered oxygen affinity requires a determination of hemoglobin oxygen dissociation curve (ODC), which relates the hemoglobin oxygen saturation to the partial pressure of oxygen in the blood. Determination of the ODC of human hemoglobin is typically carried out under conditions in which hemoglobin is in equilibrium with O2 at each partial pressure. However, in the human body due to the fast transit of RBCs through tissues hemoglobin oxygen exchanges occur under non-equilibrium conditions. We describe the determination of non-equilibrium ODC, and show that under these conditions Hb cooperativity has two apparent components in the Adair, Perutz, and MWC models of Hb. The first component, which we call sequential cooperativity, accounts for ∼70% of Hb cooperativity, and emerges from the constraint of sequential binding that is shared by the three models. The second component, which we call conformational cooperativity, accounts for ∼30% of Hb cooperativity, and is due either to a conformational equilibrium between low affinity and high affinity tetramers (as in the MWC model), or to a conformational change from low to high affinity once two of the tetramer sites are occupied (Perutz model).

Myoglobin oxygen dissociation by multiwavelength spectroscopy

1997 ◽  
Vol 82 (1) ◽  
pp. 86-92 ◽  
Author(s):  
Kenneth A. Schenkman ◽  
David R. Marble ◽  
David H. Burns ◽  
Eric O. Feigl
Keyword(s):  
Least Squares ◽  
Hill Equation ◽  
Oxygen Binding ◽  
Dissociation Curve ◽  
Nitrogen Gas ◽  
Binding Characteristics ◽  
Oxygen Fraction ◽  
Oxygen Dissociation ◽  
Dissociation Curves ◽  
The Hill

Schenkman, Kenneth A., David R. Marble, David H. Burns, and Eric O. Feigl. Myoglobin oxygen dissociation by multiwavelength spectroscopy. J. Appl. Physiol. 82(1): 86–92, 1997.—Multiwavelength optical spectroscopy was used to determine the oxygen-binding characteristics for equine myoglobin. Oxygen-binding relationships as a function of oxygen tension were determined for temperatures of 10, 25, 35, 37, and 40°C, at pH 7.0. In addition, dissociation curves were determined at 37°C for pH 6.5, 7.0, and 7.5. Equilibration was achieved with a myoglobin solution, at the desired temperature and pH, and 16 oxygen-nitrogen gas mixtures of known oxygen fraction. Correction for the inevitable presence of metmyoglobin was made by using a three-component least squares analysis and by correcting the end point oxymyoglobin spectra for the presence of metmyoglobin. The[Formula: see text] at which myoglobin is half-saturated with O2(P50) was determined to be 2.39 Torr at pH 7.0 and 37°C. The myoglobin dissociation curve was well fit by the Hill equation [saturation =[Formula: see text]/([Formula: see text]+ P50)].

scholarly journals THE HEMOGLOBIN OF THE SEA LAMPREY, PETROMYZON MARINUS

1951 ◽  
Vol 35 (1) ◽  
pp. 45-53 ◽  
Author(s):  
George Wald ◽  
Austen Riggs
Keyword(s):  
Petromyzon Marinus ◽  
Oxygen Affinity ◽  
Sea Lamprey ◽  
Oxygen Storage ◽  
Low Oxygen ◽  
Blood Hemoglobin ◽  
Oxygen Dissociation ◽  
Vertebrate Muscle ◽  
Oxygen Equilibrium Curve ◽  
Low Oxygen Affinity

The blood hemoglobin of the sea lamprey presents a curious mixture of primitive and highly specialized properties. Like muscle hemoglobin, it has a molecular weight of about 17,000, and apparently contains a single heme. Its isoelectric point is like that of a typical invertebrate hemoglobin. Its amino acid composition is partly characteristic of invertebrate) partly of vertebrate hemoglobins (Pedersen; Roche and Fontaine). In the present experiments, the oxygen equilibrium curve of this pigment was measured at several pH's. As expected, it is a rectangular hyperbola, the first such function to be observed in a vertebrate blood hemoglobin. Other hemoglobins known to possess this type of oxygen dissociation curve—those of vertebrate muscle, the worm Nippostrongylus, and the bot-fly larva—appear to serve primarily the function of oxygen storage rather than transport. Lamprey hemoglobin on the contrary is an efficient oxygen-transporting agent. It achieves this status by having, unlike muscle hemoglobin, a relatively low oxygen affinity, and a very large Bohr effect. In these properties it rivals the most effective vertebrate blood hemoglobins.

scholarly journals Antarctic Fish Blood: Respiratory Properties and the Effects Of Thermal Acclimation

1984 ◽  
Vol 109 (1) ◽  
pp. 265-279
Author(s):  
VILHELM TETENS ◽  
RUFUS M. G. WELLS ◽  
ARTHUR L. DEVRIES
Keyword(s):  
Oxygen Affinity ◽  
Antarctic Fish ◽  
Thermal Acclimation ◽  
Temperate Species ◽  
Molar Ratio ◽  
Oxygen Binding ◽  
Blood Oxygen ◽  
Low Oxygen ◽  
Blood Oxygen Affinity

1. The effects of thermal acclimation on whole blood oxygen affinity were examined in the antarctic fish Pagothenia borchgrevinki. 2. 4.5°C-acclimated fish had a P50 value of 26.7 mmHg at pH 8.1, compared to 20.7 mmHg for −1.5°C-acclimated fish. The apparent heat of oxygenation, ΔH = −26.7 kJ mol−1, is comparable to values for temperate species. 3. Warm-acclimation was followed by an increased ATP: Hb4 molar ratio, resulting in an augmentation of the thermal effect on oxy-haemoglobin affinity. This may be considered adaptive in a constantly well oxygenated environment, where oxygen loading at the gills is secured. Unloading to the tissues is thereby enhanced, supporting an elevated rate of aerobic metabolism at higher temperatures. 4. In vivo blood pH was high, between 8.10 and 8.25 at −1.5°C. Astrup titration revealed arterial CO2 tensions of less than 0.8 mmHg, indicating relative hyperventilation and low oxygen extraction efficiency in antarctic fish. 5. Blood oxygen affinities of four antarctic nototheniid species were low (P50 between 11.9 and 20.7 mmHg at pH 8.1 and --1.5°C) in comparison with the temperate species Notothenia angustata (P50 = 10.8 mmHg). The zoarcid Rhigophila dearborni had a high blood oxygen affinity (P50 = 4.3 mmHg). Blood oxygen-binding properties are discussed in relation to the polar environment, mode of life, and the concept of cold adaptation.

Physiological variation of mouse haemoglobins

1983 ◽  
Vol 218 (1213) ◽  
pp. 443-453 ◽  
Keyword(s):  
Natural Populations ◽  
Oxygen Affinity ◽  
Strain Differences ◽  
Inbred Strains ◽  
Oxygen Binding ◽  
Differential Survival ◽  
Oxygen Dissociation ◽  
The Mean ◽  
Oxygen Carrying Capacity ◽  
Β Chain

Polymorphism at Hbb (haemoglobin β-chain) is widespread in natural populations of the house mouse, Mus musculus , and appears to be maintained by natural selection. This report is an attempt to correlate genotypic fluctuations at Hbb with a most important physiological attribute of haemoglobin, its oxygen carrying capacity. Oxygen affinity has been studied and P 50 values have been measured in 12 inbred strains as well as wild-caught mice from Skokholm island. The mean P 50 of each inbred strain is a constant characteristic, although there is high within-strain variation and the oxygen affinity of the blood of an individual can fluctuate considerably from week to week. The causes of this variation remain obscure but neither within-strain nor between-strain differences are correlated with known modulators of oxygen binding. In general, the blood of mice of inbred strains as well as wild-caught mice that are homozygous for Hbb d tends to have a higher oxygen affinity than that from comparable animals homozygous for Hbb 8 , but it seems likely that the oxygen dissociation properties of haemoglobin are not the only ones important in determining differential survival of a particular Hbb type under varying environmental stress.

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