超氧化物介导的铁从铁蛋白向转铁蛋白和乳铁蛋白的转移。
The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin.
作者信息
Monteiro H P, Winterbourn C C
机构信息
Department of Pathology, Christchurch School of Medicine, Christchurch Hospital, New Zealand.
出版信息
Biochem J. 1988 Dec 15;256(3):923-8. doi: 10.1042/bj2560923.
Abstract
By the use of gel filtration and [59Fe]ferritin, apotransferrin and apolactoferrin were shown to take up iron released from ferritin by superoxide generated by hypoxanthine and xanthine oxidase. Apotransferrin also inhibited uptake of released iron by ferrozine. Ferritin and the xanthine oxidase system induced lipid peroxidation in phospholipid liposomes. This peroxidation was inhibited by apotransferrin or apolactoferrin. Thus, although superoxide and other free radicals can release iron from ferritin, either iron-binding protein, if present, should take up this iron and prevent its catalysing subsequent oxidative reactions.
摘要
通过凝胶过滤和[59Fe]铁蛋白的使用，脱铁转铁蛋白和脱铁乳铁蛋白被证明能够摄取由次黄嘌呤和黄嘌呤氧化酶产生的超氧化物从铁蛋白中释放出的铁。脱铁转铁蛋白还抑制了亚铁嗪对释放出的铁的摄取。铁蛋白和黄嘌呤氧化酶系统在磷脂脂质体中诱导脂质过氧化。这种过氧化反应受到脱铁转铁蛋白或脱铁乳铁蛋白的抑制。因此，尽管超氧化物和其他自由基能够从铁蛋白中释放铁，但如果存在任何一种铁结合蛋白，它们都应该摄取这种铁并防止其催化随后的氧化反应。
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本文引用的文献
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