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.

An electrolytic method for determining oxygen dissociation curves using small blood samples: the effect of temperature on trout and human blood

1976 ◽  
Vol 65 (1) ◽  
pp. 21-38
Author(s):  
G. M. Hughes ◽  
J. G. O'Neill ◽  
W.J. van Aardt
Keyword(s):  
Human Blood ◽  
Marked Effect ◽  
Effect Of Temperature ◽  
Oxygen Dissociation Curve ◽  
Dissociation Curve ◽  
Oxygen Dissociation ◽  
Fish Blood ◽  
Bohr Factor ◽  
Dissociation Curves ◽  
The Relationship

1. A detailed account is given of an electrolytic method for determining the oxygen dissociation curve of fish blood using a single sample of 50–100 mul for the whole curve. The accuracy and some of the problems arising from its uses are discussed. 2. Oxygen dissociation curves have been determined for trout blood and human blood at temperatures of 15 and 37 degrees C. The relationship between P50 and temperature is similar to that obtained using other methods. Absolute values of P50 are generally lower than those obtained by other methods, especially in the case of fish blood. 3. The effect of PCO2 and pH on the oxygen dissociation curve of trout blood is tested and it is shown that PCO2 has a more marked effect than pH when the other factor is maintained at a constant level. The Bohr factor (delta log P50/delta pH) appears to be approximately the same and independent of the PCO2. 4.The P50 of ray blood determined from fish during and after an operation showed an increased Bohr factor.

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

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 Oxygen dissociation curves of the blood of larval and adult lampreys (Lampetra fluviatilis)

1976 ◽  
Vol 65 (2) ◽  
pp. 449-458
Author(s):  
D. J. Bird ◽  
P. L. Lutz ◽  
I. C. Potter
Keyword(s):  
Lampetra Fluviatilis ◽  
A Value ◽  
Oxygen Dissociation ◽  
Delivery Pressure ◽  
Sedentary Animal ◽  
Ph Range ◽  
The Right ◽  
Dissociation Curves ◽  
The Hill ◽  
Hill Plots

1. An electrolytic method was used to plot the oxygen dissociation curves of whole blood from both the larva and adult of the lamprey Lampetra fluviatilis at a temperature of 10 degrees C and over a pH range of 6-5-8-1. 2. Larval blood has a far higher affinity for oxygen than that of adults, the respective calculated P50's at a pH of 7–75 being 1-9 and 10-7 mmHg. 3. The high affinity of larval blood is of use to a relatively sedentary animal living in burrows, and the increased oxygen delivery pressure brought about by the shift of the curve to the right in the adult is of advantage to an animal exhibiting greater activity. 4. The n value obtained from the Hill plots increased with increasing saturation and were lower in larvae than adults at the same level of blood saturation. 5. The Bohr effect in larvae at 10 degrees C over the pH range 6-5-8-1 was --0-25, a value which did not differ significantly from the −0-22 found in adults.

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.

Effects of Heparin Oligosaccharides with High Affinity for Antithrombin III in Experimental Venous Thrombosis

1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
Author(s):  
D P Thomas ◽  
Rosemary E Merton ◽  
T W Barrowcliffe ◽  
L Thunberg ◽  
U Lindahl
Keyword(s):  
Antithrombin Iii ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Xa ◽  
Blood Levels ◽  
Thrombin Time ◽  
High Affinity ◽  
Very High

SummaryThe in vitro and in vivo characteristics of two oligosaccharide heparin fragments have been compared to those of unfractionated mucosal heparin. A decasaccharide fragment had essentially no activity by APTT or calcium thrombin time assays in vitro, but possessed very high specific activity by anti-Factor Xa assays. When injected into rabbits at doses of up to 80 ¼g/kg, this fragment was relatively ineffective in impairing stasis thrombosis despite producing high blood levels by anti-Xa assays. A 16-18 monosaccharide fragment had even higher specific activity (almost 2000 iu/mg) by chromogenic substrate anti-Xa assay, with minimal activity by APTT. When injected in vivo, this fragment gave low blood levels by APTT, very high anti-Xa levels, and was more effective in preventing thrombosis than the decasaccharide fragment. However, in comparison with unfractionated heparin, the 16-18 monosaccharide fragment was only partially effective in preventing thrombosis, despite producing much higher blood levels by anti-Xa assays.It is concluded that the high-affinity binding of a heparin fragment to antithrombin III does not by itself impair venous thrombogenesis, and that the anti-Factor Xa activity of heparin is only a partial expression of its therapeutic potential.

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