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J Appl Physiol 41: 893-899, 1976;
8750-7587/76 $5.00
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Journal of Applied Physiology, Vol 41, Issue 6 893-899, Copyright © 1976 by American Physiological Society

ARTICLES

Influence of carbon monoxide on hemoglobin-oxygen binding

M. P. Hlastala, H. P. McKenna, R. L. Franada and J. C. Detter

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 the alpha-chain of hemoglobin. The results also suggest that heme-heme interaction is different for oxygen than for carbon monoxide.


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E. N. Bruce and M. C. Bruce
A multicompartment model of carboxyhemoglobin and carboxymyoglobin responses to inhalation of carbon monoxide
J Appl Physiol, September 1, 2003; 95(3): 1235 - 1247.
[Abstract] [Full Text] [PDF]


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