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) 的结合会降低氧含量 亲和力。 存在几个氯离子结合位点，其中只有 最高亲和力位点对氧结合不敏感。 一 提案将氧化不稳定氯化物结合位点定位在附近 Hb 的四个 α-NH(2) 末端残基。 这些网站也位于 CO(2) 作为氨基甲酸盐的结合有助于 CO(2) 运输。 这 CO(2) 结合和/或氯离子结合到相同的变构效应子 位点降低血红蛋白的氧亲和力。 带差速器 量热法和 (13)C NMR、CO(2) 与等离子结合的焓 已发现脱氧血红蛋白是氯化物浓度的函数。在 此外，氯化物与等离子脱氧Hb 结合的焓为 检查以表征α-NH(2)-末端残基结合 网站。