Respiratory functions of blood of the yak, llama, camel, Dybowski deer, and African elephant

1963 ◽  
Vol 205 (2) ◽  
pp. 331-336 ◽  
Author(s):  
Heinz Bartels ◽  
Peter Hilpert ◽  
Klaus Barbey ◽  
Klaus Betke ◽  
Klaus Riegel ◽  
...  
Keyword(s):  
Respiratory Function ◽  
African Elephant ◽  
Red Cells ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
High Concentration ◽  
Blood Samples ◽  
High Affinity ◽  
Oxygen Dissociation ◽  
Oxygen Capacity

Blood samples from a yak, llama, camel, deer, and African elephant were analyzed for oxygen capacity, "standard bicarbonate" content, oxygen dissociation curve, and the magnitude of the Bohr and Haldane effects. These parameters of the respiratory function of the blood have been related to the morphology of the red cells, to the weights of the animals, and to the most important electrolytes in the erythrocytes and in the plasma. The high affinity for oxygen described previously for llama blood is shared by its relative, the camel. Both these animals have a high concentration of hemoglobin within their erythrocytes. Blood from the African elephant showed the greatest affinity for oxygen among the subjects studied.

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).

Oxygen dissociation curve for chorioallantoic capillary blood of chicken embryo

1976 ◽  
Vol 40 (3) ◽  
pp. 393-398 ◽  
Author(s):  
H. Tazawa ◽  
T. Ono ◽  
M. Mochizuki
Keyword(s):  
Oxygen Affinity ◽  
Capillary Blood ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
Oxygen Dissociation ◽  
Oxygen Capacity ◽  
Bohr Factor ◽  
Hill’S Equations ◽  
Dissociation Curves ◽  
Clear Relation

Oxygen dissociation curves for blood in the chorioallantoic capillary of chicken embryos were determined using a microphotometric apparatus made for measuring the reaction velocity of a red blood cell with oxygen and carbon monoxide. The modified Hill's equations expressing the dissociation curve during development were calculated by two methods. P50's at pH of 7.4 were found to be 60.0, 54.4, 46.2, 33.1, and 28.6 mmHg for 10, 12, 14, 16 and 18 days of incubation, respectively. Although the Bohr factor did not show a clear relation to age, the oxygen affinity and the oxygen capacity tended to increase with the lapse of days, and the power of heme-to-heme interaction, to decrease with age. The findings imply that there is a respiratory adaptation of embryos during development.

Oxygen in acute myocardial infarction

1977 ◽  
Vol 15 (3) ◽  
pp. 10-12
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Hyperbaric Oxygen ◽  
Arterial Oxygen ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
High Concentration ◽  
Final Size ◽  
Oxygen Dissociation

In most patients with acute myocardial infarction arterial oxygen tension is reduced.1 Because of the shape of the oxygen dissociation curve the fall in oxygen saturation is probably insignificant. The practice of giving oxygen aims to correct this hypoxaemia2 so enhancing delivery of oxygen to the surrounding ischaemic area and limiting the final size of the infarct,3 preventing arrhythmias4 and relieving pain.5 Whether the inhalation of a high concentration of oxygen helps is not clear. Marginal benefits have been claimed after hyperbaric oxygen6 but this is expensive and not generally available.

scholarly journals THE TRANSPORT OF GAS BY THE BLOOD OF THE TURTLE

1926 ◽  
Vol 9 (4) ◽  
pp. 387-403 ◽  
Author(s):  
F. C. Southworth ◽  
A. C. Redfield
Keyword(s):  
Carbon Dioxide ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
High Concentration ◽  
Oxygen Dissociation ◽  
Mammalian Blood ◽  
Chemical Factors ◽  
Exact Shape ◽  
Carbon Dioxide Dissociation Curve ◽  
Carbon Dioxide Combining Power

The chief characteristics of the blood of the turtle Pseudemys concinna, considered as a system for the transport of oxygen and carbon dioxide, are its low corpuscular content (10 to 22 per cent by volume) and its high concentration of base bound as bicarbonate. These characteristics account fully for the shape and position of the carbon dioxide dissociation curve, the effect of oxygenation and reduction of the hemoglobin upon the carbon dioxide-combining power of the blood, and the distribution of carbon dioxide between the corpuscles and plasma. The oxygen-combining capacity of the turtle corpuscles does not differ from that of an equal volume of human erythrocytes. The oxygen dissociation curve is similar to that of mammalian blood and is affected in like manner by the quantity of carbon dioxide present. Its exact shape and position depend in part upon the number of corpuscles in the blood; in part its characteristics cannot be attributed to known chemical factors.

Red-cell 2,3-diphosphoglycerate in patients with hyperthyroidism

1980 ◽  
Vol 93 (4) ◽  
pp. 424-429 ◽  
Author(s):  
J. L. Alvarez-Sala ◽  
M. A. Urbán ◽  
J. J. Sicilia ◽  
A. J. Diaz Fdez ◽  
F. Fdez Mendieta ◽  
...  
Keyword(s):  
Thyroid Hormones ◽  
Control Group ◽  
Red Cell ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
Oxygen Dissociation ◽  
The Right ◽  
Serum Thyroid Hormones ◽  
Hyperthyroid Patients ◽  
2,3 Dpg

Abstract. In 21 hyperthyroid female patients studied on 29 occasions, high levels of red-cell 2,3-diphosphoglycerate (2,3-DPG) have been found (5.75 ± 0.7 mm) which, compared to a euthyroid control group (4.88 ± 0.4 mm), could not be accounted for by differences in haematocrit, haemoglobin or phosphataemia. A significant correlation was found (P < 0.05) between serum thyroid hormones and the 2,3-DPG concentration in the hyperthyroid patients. Eight of these patients were reexamined after treatment and normalization of thyroid function, showed a regression to normal 2,3-DPG values (4.81 ± 0.6 mm) which could not be attributed to variations in haematocrit, haemoglobin or phosphataemia either. We therefore deduce that the shift to the right in the haemoglobin oxygen dissociation curve observed in patients of this type may be due to an increase in the red-cell 2,3-DPG content.

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