[Determination of the standard oxyhemoglobin dissociation curve in horses. Effects of temperature, pH and diphosphoglycerate].
Abstract: The equine blood oxyhemoglobin dissociation curve has been traced in its entirety in standard conditions and the effects of temperature, pH and 2,3-diphosphoglycerate on this curve have been measured. When compared to that of human blood, the curve showed a higher oxygen affinity of hemoglobin (23.8 +/- 0.8 versus 26.6 mm Hg). The effect of the pH, expressed by d log P50/dpH, was found to be identical in man and horse (-0.47). The effect of temperature, however, expressed by d log P50/dT, proved to be lower in the horse (0.016 versus 0.024). The P50 showed an increase of 1 mm Hg each time 2,3-diphosphoglycerate was experiencing an elevation of 4 mumol/gHb in the horse. The results obtained from this experiment are intended for the replacement of the values related to the human blood which have been found to be somewhat inadequate for the horse blood, when the data of blood gases are given in algorithms. The equine blood oxyhemoglobin dissociation curve has been traced in its entirety in standard conditions and the effects of temperature, pH and 2,3-diphosphoglycerate on this curve have been measured. When compared to that of human blood, the curve showed a higher oxygen affinity of hemoglobin (23.8 +/- 0.8 versus 26.6 mm Hg). The effect of the pH, expressed by d log P50/dpH, was found to be identical in man and horse (-0.47). The effect of temperature, however, expressed by d log P50/dT, proved to be lower in the horse (0.016 versus 0.024). The P50 showed an increase of 1 mm Hg each time 2,3-diphosphoglycerate was experiencing an elevation of 4 mumol/gHb in the horse. The results obtained from this experiment are intended for the replacement of the values related to the human blood which have been found to be somewhat inadequate for the horse blood, when the data of blood gases are given in algorithms.
Publication Date: 1986-04-01 PubMed ID: 3756672PubMed Central: PMC1255188
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- Comparative Study
- English Abstract
- Journal Article
Summary
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This study analyses the standard oxyhemoglobin dissociation curve in horses with an emphasis on the impact of temperature, pH, and the concentration of 2,3-diphosphoglycerate. The research indicates a higher affinity for oxygen in equine hemoglobin compared to human, and tracks changes in certain conditions which can influence the way blood gases data are interpreted for horses.
Equine vs Human Oxyhemoglobin Dissociation Curve
- The research primarily focuses on the oxyhemoglobin dissociation curve of horse blood under standard conditions.
- This curve demonstrates the degree of oxygen saturation as a function of varied oxygen tensions and helps in understanding how readily oxyhemoglobin releases its oxygen.
- Against human blood’s dissociation curve, the equine curve shows a higher oxygen affinity – the measure of how tightly the oxygen is bound to hemoglobin.
- For humans, the affinity is noted at 26.6 mm Hg, while it is 23.8 +/- 0.8 mm Hg for horses – signifying that hemoglobin in horse blood binds oxygen more tightly.
Effects of pH and Temperature
- The effect of pH on the P50 (partial pressure of oxygen when hemoglobin is 50% saturated) showed identical results in humans and horses, represented by d log P50/dpH equating to -0.47.
- However, the temperature impact differed as horses showed lesser P50 temperature dependence than humans. The value for horses stood at 0.016 as compared to 0.024 in humans, indicating that the ability of hemoglobin to carry oxygen in horses wouldn’t change as much with fluctuations in body temperature.
2,3-Diphosphoglycerate (DPG) influence
- The study also examined the impact of changes in 2,3-diphosphoglycerate levels on P50 in equine blood.
- DPG is an organophosphate that influences oxygen affinity in hemoglobin, meaning any change in DPG levels can affect how readily hemoglobin binds and releases oxygen.
- The P50 increased by 1 mm Hg every time there was a rise of 4 mumol/gHb in DPG levels in horse blood. This suggests DPG has a critical role to play in regulating oxygen delivery in the equine system.
Study Significance
- The findings provide a better understanding of blood gases’ data interpretation for equine blood, challenging the adequacy of human blood related values in such readings.
- The research underscores the need to take the unique properties of equine blood into account when tracking and analyzing blood gases in horses, potentially leading to more accurate medical diagnoses and interventions.
Cite This Article
APA
Clerbaux T, Serteyn D, Willems E, Brasseur L.
(1986).
[Determination of the standard oxyhemoglobin dissociation curve in horses. Effects of temperature, pH and diphosphoglycerate].
Can J Vet Res, 50(2), 188-192.
Publication
Researcher Affiliations
MeSH Terms
- 2,3-Diphosphoglycerate
- Animals
- Diphosphoglyceric Acids / blood
- Female
- Horses / blood
- Humans
- Hydrogen-Ion Concentration
- Male
- Oxygen / blood
- Oxyhemoglobins / analysis
- Reference Standards
- Regression Analysis
- Sex Factors
- Temperature
References
This article includes 6 references
- Severinghaus JW. Blood gas calculator.. J Appl Physiol 1966 May;21(3):1108-16.
- Benesch RE, Benesch R, Yu CI. The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration.. Biochemistry 1969 Jun;8(6):2567-71.
- van KAMPEN E, ZIJLSTRA WG. Standardization of hemoglobinometry. II. The hemiglobincyanide method.. Clin Chim Acta 1961 Jul;6:538-44.
- Bunn HF, Kitchen H. Hemoglobin function in the horse: the role of 2,3-diphosphoglycerate in modifying the oxygen affinity of maternal and fetal blood.. Blood 1973 Sep;42(3):471-9.
- Sottiaux B, Clerbaux T, Fesler R, Brohet C. Computer processing of oxygen dissociation curves.. Comput Programs Biomed 1976 Oct;6(3):128-35.
- Clerbaux T, Fesler R, Bourgeois J. A dynamic method for continuous recording of the whole blood oxyhemoglobin dissociation curve at constant temperature, pH and P CO2 .. Med Lab Technol 1973 Jan;30(1):1-9.
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