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Hemoglobin-oxygen affinity in anemia

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Summary

In blood of 21 anemic patients and 8 normal subjects (N) thre oxygen dissociation curves each were measured at different pH values to calculate Bohr coefficients after acidification with CO2 (BCCO 2) or fixed acid (BCFA), and other important parameters of oxygen affinity. The patients had either low hemoglobin or red cell production (L:n=11, 7.3 g/dl Hb) or high erythrocyte production combined with high loss (H:n=10, 7.8 g/dl Hb). The standard half saturation pressure P50 (pH 7.4, 37°C) was equally elevated in both anemic groups (L:30.5, H:30.8, N:26.7 mmHg), as well as the diphosphoglycerate concentration (DPG) (L:18.7, H:18.6, N:12.7 μmol/g Hb). The red cell pH of the anemics was lower than for the N (approximately 0.045 units) causing part of the difference in P50. Hill's “n”tended to high values in the anemics except at low O2-saturation in the H. For BCCO 2 no significant difference among the groups was observed. BCFA, however, increased in the H at low SO 2 compared to the N and L. The cause for most of the changes in hemoglobin oxygen affinity in anemics was the high [DPG]. The combination of high P50 and high “n” value as in the L seems to be most advantageous for tissue oxygenation.

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The measurements were performed during a stay as visiting professor at the Universidad del Valle, supported by Deutscher Akademischer Austauschdienst VS 931 509 0013

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Böning, D., Enciso, G. Hemoglobin-oxygen affinity in anemia. Blut 54, 361–368 (1987). https://doi.org/10.1007/BF00626019

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