DEVELOPMENT OF BIOPHYSICAL METHODS FOR STUDYING BIOCHEMICAL REACTIONS

研究生化反应的生物物理方法的发展

• 批准号: 3779534
• 负责人: R L BERGER
• 金额: --
• 依托单位: NATIONAL HEART, LUNG, AND BLOOD INSTITUTE
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3779534
• 关键词: biophysics; calorimetry; carbon dioxide; chemical binding; chemical reaction; chlorine; hemoglobin; method development; nuclear magnetic resonance spectroscopy; oxygen

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.

氯化物和/或CO（2）与血红蛋白（Hb）的结合降低了氧含量。 亲和力 氯离子有几个结合位点，其中只有 最高亲和力位点对氧结合不敏感。 一 建议在附近找到一个不稳定的氯化物结合位点， Hb的四个α-NH（2）末端残基。 这些网站也是 CO（2）以氨基甲酸酯的形式结合有助于CO（2）的运输。 的 CO（2）结合和/或氯离子结合至相同的变构效应物 位点降低血红蛋白的氧亲和力。 具有差分 量热法和（13）C NMR，CO（2）结合到等离子体的焓 已发现脱氧血红蛋白是氯化物浓度的函数。在 此外，氯离子结合到等离子脱氧血红蛋白的焓已被 检查以表征α-NH（2）-末端残基结合 网站.