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INTERACTIONS OF MODIFIED HEMOGLOBINS WITH IRON CHELATORS

INTERACTIONS OF MODIFIED HEMOGLOBINS WITH IRON CHELATORS
修饰血红蛋白与铁螯合剂的相互作用
批准号:
3804885
负责人:
A I ALAYASH
金额:
$0.0万
依托单位国家:
美国
项目类别:
财政年份:
--
资助国家:
美国
项目状态:
未结题
起止时间:
至

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中文摘要
翻译
在目前旨在减少苯系物氧化作用的策略中 HBOCs是利用铁络合剂防止潜在的分子 铁诱导的氧自由基引起的细胞损伤。我们 去铁胺与新铁胺相互作用的研究 开发的吡喃酮(乙基麦芽酚)的自氧化和氢化速率 过氧化氢介导的交联血红蛋白的氧化。有一个 自氧化和半铬的速率都略有下降 乙基麦芽糖醇加入培养基时的形成 这些血红蛋白。相反,纳入去铁胺会导致 氧化产物增多。在反应混合物中,在 存在过多的过氧化氢,去铁胺导致20-30% 高铁血红蛋白升高,同时半红细胞轻微减少 队形。另一方面,乙基麦芽酚几乎没有或几乎没有作用。 与乙基麦芽酚不同,去铁胺在以下情况下是独立的 铁的作弊特性,起到了氧化剂的作用。这可能与 其与氧自由基直接相互作用的能力 高铁血红蛋白的形成增加。计划进行进一步的研究 验证这一点,并研究其潜在的分子机制 去铁胺的作用。
英文摘要
Among the current strategies aimed at decreasing the oxidant effect of HBOCs is the use of iron chelators to prevent the potential molecular and cellular damage caused by iron induced oxygen free radicals. We studies the effects of interactions of desferrioxamine and newly developed pyrone (ethyl maltol) on the rate of autoxidation and hydrogen peroxide mediated oxidation of crosslinked hemoglobins. There was a slight decrease in both the rate of autoxidation and hemichrome formation when ethyl maltol was included in the incubation media of these hemoglobins. Conversely, inclusion of desferrioxamine led to an increase in oxidation products. In the reaction mixture, and in the presence of excess hydrogen peroxide, desferrioxamine led to a 20-30% rise in methemoglobin coupled with slight reduction in the hemichrome formation. Ethyl maltol, on the other hand, had little or no effect. It appears that unlike ethyl maltol, desferrioxamine independent if its iron cheating properties, acts as an oxidizing agent. This may relate to its ability to interact directly with oxygen free radicals resulting in increased methemoglobin formation. Further studies are planned to verify this and to investigate the underlying molecular mechanism of desferrioxamine's action.
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SEPARATION AND CHARACTERIZATION OF ALTERED HEME PRODUCTS
  • 批准号:
    3770431
  • 项目类别:
  • 资助金额:
    $0.0万
  • 财政年份:
    --
  • 负责人:
    A I ALAYASH
  • 依托单位:
    --
MODIFIED HEMOGLOBINS AS A SOURCE OF ACTIVATED OXYGEN SPECIES
AUTOOXIDATION AND STABILITY OF CROSSLINKED HEMOGLOBINS
FUNCTIONAL MODIFICATIONS OF SICKLE CELL ERYTHROCYTES