Independence of Whole Blood and HÆmoglobin Solution Oxygen Dissociation Curves from HÆmoglobin Type

Nature ◽  
1962 ◽  
Vol 196 (4854) ◽  
pp. 550-553 ◽  
Author(s):  
J. J. P. SCHRUEFER ◽  
C. J. HELLER ◽  
F. C. BATTAGLIA ◽  
A. E. HELLEGERS
Keyword(s):  
Whole Blood ◽  
Oxygen Dissociation ◽  
Haemoglobin Type ◽  
Haemoglobin Solution ◽  
Dissociation Curves

scholarly journals The effect of temperature on the oxygen dissociation curves of whole blood of larval and adult lampreys (Geotria australis)

1982 ◽  
Vol 97 (1) ◽  
pp. 253-261
Author(s):  
D. J. Macey ◽  
I. C. Potter
Keyword(s):  
Whole Blood ◽  
Life Cycle Stage ◽  
Effect Of Temperature ◽  
High Affinity ◽  
Oxygen Dissociation ◽  
Geotria Australis ◽  
Oxygen Tensions ◽  
Dissociation Curves ◽  
Hill Plots ◽  
Very High

1. Oxygen dissociation curves of the whole blood of larvae and adults of the Southern Hemisphere lamprey Geotria australis have been determined between pH 6.8 and 8.2 at 5, 15 and 25 degrees C. 2. The P50's at temperatures of 5, 15 and 25 degrees C and a pH of 7.75 were respectively 0.57, 0.92 and 1.19 mmHg in larvae and 6.9, 10.3 and 19.0 mmHg in adults. 3. The relatively very high affinity of larval blood for oxygen may reflect an adaptation to low environmental oxygen tensions. 4. The Bohr shift was not significantly affected by either temperature or life-cycle stage. 5. The slope (n) in Hill plots increased with temperature and oxygen saturation, and was greater in adults than in larvae.

scholarly journals Haemoglobin and Erythrocyte Potassium Types in Sheep and their Influence on Oxygen Dissociation and Haemoglobin Denaturation

1962 ◽  
Vol 15 (2) ◽  
pp. 371 ◽  
Author(s):  
TJ Dawson ◽  
JV Evans
Keyword(s):  
Potassium Concentration ◽  
Oxygen Dissociation ◽  
Haemoglobin Type ◽  
Dissociation Curves

The influence of haemoglobin type and erythrocyte potassium concentration on oxygen dissociation curves and rate of denaturation of haemoglobin by alkali have been studied in Southdown sheep.

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.

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.

scholarly journals Reliability of the determination of whole-blood oxygen affinity by means of blood-gas analyzers and multi-wavelength oximeters.

1989 ◽  
Vol 35 (5) ◽  
pp. 773-777 ◽  
Author(s):  
G Kwant ◽  
B Oeseburg ◽  
W G Zijistra
Keyword(s):  
Whole Blood ◽  
Carbon Monoxide Poisoning ◽  
Oxygen Affinity ◽  
Reference Interval ◽  
Accurate Method ◽  
Blood Gas ◽  
Oxygen Dissociation ◽  
Multi Wavelength ◽  
Dissociation Curves

Abstract Determination of the oxygen affinity of human whole blood with the help of blood-gas analyzers and multi-wavelength oximeters is compared with an accurate method for recording hemoglobin oxygen dissociation curves (Clin Chem 1982;28:1287-92). P50 (oxygen tension at half saturation; So2 = 50%) and Hill's n (delta log [So2/(1-So2)]/delta log Po2) were determined in blood of 24 healthy donors. Three slightly different procedures were used for determination of P50 on the basis of Po2, pH, Pco2, and So2 measured with each of four different blood-gas analyzer/oximeter combinations. These methods were not able to discriminate between high and low values for P50 within the normal reference interval, but never failed to detect the high oxygen affinity of blood stored for 12 days, reflected in low values of P50. The methods thus proved suitable for detecting clinically significant deviations in oxygen affinity such as occur in patients with, e.g., abnormal hemoglobins, anemias, or carbon monoxide poisoning. Determination of Hill's n by these methods did not produce useful results.

Oxygen dissociation curves for whole blood, recorded with an instrument that continuously measures pO2 and sO2 independently at constant t, pCO2, and pH.

1982 ◽  
Vol 28 (6) ◽  
pp. 1287-1292 ◽  
Author(s):  
A Zwart ◽  
G Kwant ◽  
B Oeseburg ◽  
W G Zijlstra
Keyword(s):  
Whole Blood ◽  
Data Acquisition System ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
Measuring Chamber ◽  
Oxygen Dissociation ◽  
Constant Determination ◽  
Blood Specimens ◽  
Dissociation Curves

Abstract We describe a method for recording oxygen dissociation curves for whole-blood specimens. The blood sample is placed in a thermostated measuring chamber, and pO2 and SO2 are measured continuously by polarography and by reflectometry, respectively. During the recording of an oxygen dissociation curve, the pO2 and SO2 signals are stored in a data-acquisition system, while pH, pCO2, and temperature are kept constant. Determination of precision and error discussion indicated that the coefficient of variation (CV) of the determination of the oxygen dissociation curve is mainly determined by the error in the measurement of SO2. The overall CV of pO2 values belonging to the lower, mid-, and upper parts of the SO2 range is estimated to be about 2.6, 3.1, and 2.1%, respectively. In practice the measurements are about 30% more precise than estimated. With our method, the fixed-acid-induced Bohr effect (H+ factor) can be determined over the entire SO2 range with much greater precision than hitherto.

The oxygen dissociation curve of haemoglobin in dilute solution

1936 ◽  
Vol 120 (819) ◽  
pp. 484-495 ◽  
Keyword(s):  
Spectroscopic Method ◽  
Marked Change ◽  
Maternal Blood ◽  
Gas Analysis ◽  
Dilute Solution ◽  
Dissociation Curve ◽  
Foetal Haemoglobin ◽  
Oxygen Dissociation ◽  
Dissociation Curves ◽  
The Relationship

The spectroscopic determination of the oxygen dissociation curves of haemoglobin has an advantage over the tonometer and gas analysis method, in that much smaller quantities of haemoglobin can be made use of. The spectroscopic method was used to determine the relationship between the foetal and maternal haemoglobins in the sheep during a study of foetal respiration made by Barcroft (1935). The conditions for the comparison of the haemoglobins were a dilute solution of the haemoglobin at p H 9·2 (borate buffer) and at 20° C. These conditions were chosen because of the very accurate determinations of the dissociation curves of dilute haemoglobin of the sheep by Forbes and Roughton (1931) and because these authors recommend p H 9·2 at room temperature as most suitable for a study of the oxygen equilibrium of haemoglobin, all the haemoglobin being in the form of the alkali salt. McCarthy (1933) and Hall (1934) had found previously that the haemoglobins of the foetal and maternal goat were different, the foetal haemoglobin (in the blood and as purified haemoglobin) having a higher affinity for oxygen. The same relationship was found to exist in the sheep haemoglobins in dilute solution at 20° C and p H 9·2. When samples of human foetal and maternal blood (sent by Professor Fleming from the Obstetrical Department of the Royal Free Hospital) were compared in dilute solution it was found that the foetal haemoglobin had a lower affinity for oxygen than the maternal. This was also found by Haurowitz (1935) for dilute solutions of the haemoglobins of mother and new born infant. Haurowitz, however, pointed out that in the corpuscles the affinity for oxygen is less in the infant’s haemoglobin than in that of the mother, but the method used by him did not allow of measurements on suspensions of corpuscles. In the present work the dissociation curves of dilute suspensions of corpuscles have been compared with similar solutions of the haemoglobin. It was found that the relationship of the dissociation curves for human foetal and maternal corpuscles is the same as that found by Barcroft in the goat and in the sheep. It has now been found that by a dilution of human adult haemoglobin the dissociation curve is altered by 200% to a position of higher affinity for oxygen, without any marked change in shape. The haemoglobin of the human foetus, on the other hand, is much less affected by dilution, thus explaining the anomaly of the reversed relationship when solutions of the haemoglobins are used instead of suspensions of corpuscles. It was shown by the work of Bock, Field, and Adair (1924), and by Adair (1925), that a solution of haemoglobin free from stromata and of a similar concentration to blood gives a dissociation curve like whole blood. This makes it clear that in the comparison of dilute haemoglobin solutions with suspensions of corpuscles we are concerned, not simply with a change in the haemoglobin due to haemolysis, but a change due to a dilution of the contents of the corpuscle.

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