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）的结合降低了氧气 亲和力。 氯化物存在几个结合位点，其中只有 最高亲和力位点对氧结合不敏感。 一 提案定位在附近的氯化氯化物结合位点 HB的四个α-NH（2） - 末端残基。 这些站点也是 CO（2）作为氨基甲酸酯的结合有助于CO（2）运输。 这 CO（2）结合和/或氯化物与相同的变构效应器结合 位点较低（S）血红蛋白的氧亲和力。 与差异 量热法和（13）c nmr，Co（2）与等元素结合的焓 已发现脱氧Hb是氯化物浓度的函数。在 此外，氯化焓与等氧基hb的结合已是 检查以表征thealpha-nh（2） - 末端残基结合 站点。