CO2 dissociation curves of concentrated human deoxy and carbon monoxyhemoglobin at 37°, pH 7.6 to 7.0, pCO2 = 10 to 160 mm Hg, have been obtained by a rapid mixing and ion exchange technique. The CO2 dissociation curves for deoxyhemoglobin can only be fitted by assuming 2 classes of binding sites for carbon dioxide. The simplest way to account for the experimental data is to assume that the α amino groups of the α and β chains react with carbon dioxide with affinities that differ by at least a factor of 3. No difference in reactivity with CO2 was found among the 4 terminal α amino groups of carbon monoxyhemoglobin.
|Number of pages||6|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - 1975|
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