• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Chemico-biological interactions >The peroxidase activity of ADM-Fe3+ cooperates with lipid peroxidation: The participation of hydroperoxide and hydroxyl radicals in the damage to proteins and DNA
【24h】

The peroxidase activity of ADM-Fe3+ cooperates with lipid peroxidation: The participation of hydroperoxide and hydroxyl radicals in the damage to proteins and DNA

机译：ADM-Fe3 +的过氧化物酶活性与脂质过氧化协同作用：氢过氧化物和羟基自由基参与对蛋白质和DNA的破坏

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

To investigate the mechanisms of cardiotoxicity induced by adriamycin (ADM), the enzymatic activities of ADM-Fe3+, including the peroxidase and lipoxygenase (LOX) activity, and participation of active oxygen species in the damage to biological components were examined. ADM-Fe3+, but not ADM, steadily oxidized tetramethyl-p-phenylenediamine in the presence of peroxides, indicating that ADM-Fe3+ acts as a peroxidase. However, the activity of ADM-Fe3+ as peroxidase was very low compared with that of heme peroxidase, but was similar to that of LOX, which has a known peroxidase activity. Conversely, the activity of ADM-Fe3+ as a LOX was also very low compared with that of LOX itself. However, the lipid hydroperoxides (LOOH) produced by ADM-Fe3+ were the substrate for ADM-Fe3+ as a peroxidase. These findings indicate that lipid peroxidation cooperates with the peroxidase activity of ADM-Fe3+. Hydroxyl radicals (HO center dot) were generated when ADM-Fe3+ was incubated with H2O2, but not with LOOH. Alcohol dehydrogenase was inactivated by LOOH. Conversely, DNA was mainly damaged by ADM-Fe3+ with H2O2. A small amount of DNA remained at the starting point on agarose gels during incubation with ADM-Fe3+ with LOOH and ADM-Fe3+ with H2O2. It seems that HO center dot and compound I-like species participate in the strand breaks and the aggregation of DNA, respectively. (C) 2015 Elsevier Ireland Ltd. All rights reserved.
机译：为了研究阿霉素（ADM）引起的心脏毒性的机制，研究了ADM-Fe3 +的酶活性，包括过氧化物酶和脂氧合酶（LOX）活性，以及​​活性氧参与对生物成分的损害。在过氧化物的存在下，ADM-Fe3 +（而不是ADM）稳定地氧化了四甲基对苯二胺，表明ADM-Fe3 +起着过氧化物酶的作用。但是，与血红素过氧化物酶相比，ADM-Fe3 +作为过氧化物酶的活性非常低，但与具有已知过氧化物酶活性的LOX相似。相反，与LOX本身相比，ADM-Fe 3+作为LOX的活性也非常低。但是，由ADM-Fe3 +产生的脂质氢过氧化物（LOOH）是ADM-Fe3 +作为过氧化物酶的底物。这些发现表明脂质过氧化与ADM-Fe 3+的过氧化物酶活性协同作用。当将ADM-Fe3 +与H2O2而不与LOOH一起孵育时，会生成羟基自由基（HO中心点）。乙醇脱氢酶被LOOH灭活。相反，DNA主要被过氧化氢的ADM-Fe3 +破坏。在与AOH-Fe3 +与LOOH和ADM-Fe3 +与H2O2孵育期间，琼脂糖凝胶的起始点处残留少量DNA。似乎HO中心点和化合物I样物质分别参与了链断裂和DNA的聚集。 （C）2015 Elsevier Ireland Ltd.保留所有权利。

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