Suppr超能文献

[白蛋白结合的二亚硝酰基铁配合物与活性氧之间的相互作用]

[Interaction between albumin-bound dinitrosyl iron complexes and reactive oxygen species].

作者信息

Shumaev K B, Gubkin A A, Gubkina S A, Gudkov L L, Lakomkin V L, Topunov A F, Vanin A F, Ruuge E K

出版信息

Biofizika. 2007 May-Jun;52(3):534-8.

Abstract

It has been established that albumin-bound dinitrosyl iron complexes can be destroyed by superoxide radicals generated in a xanthine-xanthine oxidase system. It was shown that peroxynitrite also effectively destroyed albumin-bound dinitrosyl iron complexes. At the same time, hydrogen peroxide and tert-butyl hydroperoxide did not stimulate the destruction of albumin-bound dinitrosyl iron complexes up to concentrations one order higher than the content of NO. The data have been obtained indicating that dinitrosyl iron complexes possess the vasodilatory activity. It has been proposed that peroxynitrite and superoxide radical, by causing the destruction of albumin-bound dinitrosyl iron complexes, affect the physiological properties of nitric oxide.

摘要

已经确定,白蛋白结合的二亚硝酰基铁配合物可被黄嘌呤-黄嘌呤氧化酶系统中产生的超氧自由基破坏。结果表明,过氧亚硝酸盐也能有效破坏白蛋白结合的二亚硝酰基铁配合物。同时,过氧化氢和叔丁基过氧化氢在浓度比一氧化氮含量高一个数量级之前,不会刺激白蛋白结合的二亚硝酰基铁配合物的破坏。已获得的数据表明二亚硝酰基铁配合物具有血管舒张活性。有人提出,过氧亚硝酸盐和超氧自由基通过破坏白蛋白结合的二亚硝酰基铁配合物,影响一氧化氮的生理特性。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验