Oxygen affinity of human blood in presence of carbon monoxide

1976 ◽  
Vol 40 (3) ◽  
pp. 487-490 ◽  
Author(s):  
C. R. Collier
Keyword(s):  
Carbon Monoxide ◽  
Human Blood ◽  
Oxygen Affinity ◽  
Considerable Error

If carbon monoxide is present in the blood, it is necessary to quantitate its effect on apparent O2 affinity in order to properly compute venous PO2 and P50. Ways of doing this are analyzed theoretically. The classical principles of Haldane and of Roughton and Darling are reviewed and simplified. The method of computation of PO2 in the presence of CO as introduced by Forster is shown to be in considerable error. The source of this error is determined. The error produced if the presence of CO is ignored during the computation of P50 is analyzed.

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.

A New Approach for the Carbon Monoxide (CO) Exposure Diagnosis: Measurement of Total CO in Human Blood Versus Carboxyhemoglobin (HbCO)

2013 ◽  
Vol 58 (4) ◽  
pp. 1041-1046 ◽  
Author(s):  
Vincent Varlet ◽  
Emma Lagroy De Croutte ◽  
Marc Augsburger ◽  
Patrice Mangin
Keyword(s):  
Carbon Monoxide ◽  
Human Blood ◽  
New Approach

scholarly journals Carboxyhemoglobin and oxygen affinity of human blood.

1984 ◽  
Vol 30 (7) ◽  
pp. 1250-1251 ◽  
Author(s):  
E Rovida ◽  
M Niggeler ◽  
S Carlone ◽  
M Samaja
Keyword(s):  
Human Blood ◽  
Oxygen Affinity ◽  
Temperature Range ◽  
Ph Values ◽  
Total Hemoglobin ◽  
Normal Human ◽  
Normal Human Blood

Abstract We determined normal human blood p50 at various pH values (range 7.0 to 7.6) as a function of the proportion of carboxyhemoglobin (COHb) in total hemoglobin, from 0 to 23%. The d(log p50)/d[COHb] coefficient is 0.00848, independent of pH and 2,3-diphosphoglycerate. The derived equation allows the calculation of p50 as a function of COHb with an approximation of +/- 0.54 mmHg (about 72 Pa), and can be combined with other calculations (Clin Chem 27:1856-1861, 1981; Clin Chem 29:110-114, 1983) to predict p50 under any condition of pH within the range 7.0-7.6, ratio of [2,3-diphosphoglycerate] to [total hemoglobin] (range 0.3-2.5), pCO2 (range 20-90 mmHg), temperature (range 19-43 degrees C), and COHb (range 0-23%).

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