DEVELOPMENT OF BIOPHYSICAL METHODS FOR STUDYING BIOCHEMICAL REACTIONS

氯和/或CO(2)与血红蛋白(Hb)的结合降低了氧 亲和力。氯离子有几个结合部位，其中只有 最高亲和力部位对氧结合不敏感。一 Proposal在附近找到了一个可氧氯结合的位置 Hb的四个α-NH(2)末端残基。这些地点也是 CO(2)作为氨基甲酸酯的结合有助于CO(2)的运输。这个 CO(2)与同一变构效应器的结合和/或氯结合 位置较低(S)的血红蛋白的氧亲和力。使用差分 量热法和~(13)C核磁共振法测定CO(2)与等离子的结合热 已发现脱氧血红蛋白是氯离子浓度的函数。在……里面 此外，氯与等离子脱氧Hb的结合热为 为了表征α-NH(2)末端残基结合而进行的检查 网站。

The binding of chloride and/or CO(2) to hemoglobin (Hb) lowers the oxygen affinity. Several binding sites are present for chloride, of which only the highest affinity site is not sensitive to oxygen binding. One proposal locates an oxylabile chloride binding site in the vicinity of the four alpha-NH(2)-terminal residues of Hb. These sites are also where the binding of CO(2) as carbamate contributes to CO(2) transport. The CO(2) binding and/or chloride binding to the same allosteric effector sites lower(s) the oxygen affinity of hemoglobin. With differential calorimetry and (13)C NMR, the enthalpy of CO(2) binding to isoionic deoxyHb has been found as a function of chloride concentration. In addition, the enthalpy of chloride binding to isoionic deoxyHb has been examined in order to characterize thealpha-NH(2)-terminal residue binding sites.