Hlastala M P, McKenna H P, Franada R L, Detter J C
J Appl Physiol. 1976 Dec;41(6):893-9. doi: 10.1152/jappl.1976.41.6.893.
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.
在正常全血中测量氧解离曲线和波尔效应，作为碳氧血红蛋白浓度[HbCO]的函数。通过改变二氧化碳浓度（二氧化碳波尔效应）或在恒定PCO₂下添加等渗NaOH或HCl（固定酸波尔效应）来改变pH值。当[HbCO]在2%、25%、50%和75%范围内变化时，P50分别为26.3、18.0、11.6和6.5 mmHg。二氧化碳波尔效应在低氧饱和度时最高。随着[HbCO]增加，这种效应没有改变。然而，当[HbCO]从2%增加到75%时，在极低氧饱和度下，固定酸波尔因子的幅度从-0.20增加到-0.80。在高[HbCO]时，分子二氧化碳结合（氨基甲酰）对氧亲和力的影响被消除。这些结果与氧气或一氧化碳最初与血红蛋白α链结合一致。结果还表明，血红素-血红素相互作用对于氧气和一氧化碳是不同的。
