Perrella M, Bresciani D, Rossi-Bernardi L
J Biol Chem. 1975 Jul 25;250(14):5413-8.
CO2-dissociation curves of concentrated human deoxy- and carbonmonoxyhemoglobin at 37 degrees, pH 7.6 to 7.0, PCO2 equal to 10 to 160 mm Hg, have been obtained by a rapid mixing and ion exchange technique. The CO2-dissociation curves for deoxyhemogloblin can only be fitted by assuming two classes of binding sites for carbon dioxide. The simplest way to account for the experimental data is to assume that the alpha-amino groups of the alpha and beta 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 four terminal alpha-amino groups of carbonmonoxyhemoglobin.
通过快速混合和离子交换技术，已获得在37摄氏度、pH值为7.6至7.0、二氧化碳分压等于10至160毫米汞柱条件下浓缩的人脱氧血红蛋白和碳氧血红蛋白的二氧化碳解离曲线。脱氧血红蛋白的二氧化碳解离曲线只有通过假设存在两类二氧化碳结合位点才能拟合。解释实验数据的最简单方法是假设α链和β链的α-氨基与二氧化碳反应时的亲和力至少相差3倍。在碳氧血红蛋白的四个末端α-氨基之间未发现与二氧化碳反应性的差异。
