...
首页> 外文期刊>Human physiology >Oxygenation of Native or UV-Modified Human Hemoglobin in the Presence of Nitric Oxide
【24h】

Oxygenation of Native or UV-Modified Human Hemoglobin in the Presence of Nitric Oxide

机译:一氧化氮存在下对天然或紫外线修饰的人类血红蛋白的氧化

获取原文
获取原文并翻译 | 示例
           

摘要

The effect of 0.1-10% nitrosohemoglobin (HbNO) on the functional properties of human oxyhe-moglobin (HbO_2) was studied before and after UV irradiation at 151-453 J/m~2. Oxygen binding analysis showed that HbNO intensified the first stage of oxygenation and weakened the cooperative interactions in the tetramer, decreasing the affinity of hemoglobin for oxygen at physiologically important oxygen partial pressures (40-100 mm Hg). Mixtures of HbO_2 and HbNO were highly resistant to "therapeutic" doses of UV irradiation. Since the functional activity of hemoglobin depended nonlinearly on the concentration of HbNO in the mixture, it was assumed that sophisticated interactions of HbO_2 and HbNO yielded a new product differing in properties from the initial components.
机译:研究了0.1-10%的亚硝基血红蛋白(HbNO)对人氧合-血红蛋白(HbO_2)的功能特性的影响,在151-453 J / m〜2的紫外线照射前后。氧结合分析表明,在生理重要的氧分压(40-100 mm Hg)下,HbNO增强了氧合的第一阶段,削弱了四聚体中的协同相互作用,从而降低了血红蛋白对氧的亲和力。 HbO_2和HbNO的混合物对“治疗”剂量的紫外线辐射具有高度抵抗力。由于血红蛋白的功能活性与混合物中HbNO的浓度非线性相关,因此可以假定HbO_2和HbNO的复杂相互作用产生了一种新产物,其性质与初始组分不同。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号