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分离线粒体上铁蛋白结合位点与铁蛋白中铁动员的相关性。

Relevance of ferritin-binding sites on isolated mitochondria to the mobilization of iron from ferritin.

作者信息

Ulvik R J

出版信息

Biochim Biophys Acta. 1982 Mar 15;715(1):42-51. doi: 10.1016/0304-4165(82)90047-2.

Abstract

Iron can be released from ferritin and utilized by isolated rat liver mitochondria for the synthesis of heme. Mobilization of iron from ferritin is initiated by the binding of ferritin to the mitochondria in an manner compatible with binding sites or receptors for ferritin on the mitochondria. The binding completes rapidly, it is independent of temperature, saturable, reversible and enhanced by K+ and Mg2+. The amount of ferritin binding sites is approx. 0.8 pmol/mg mitochondrial protein, and the affinity constant is 6.4 . 10(6)M-1. The binding kinetics correlate well with the functional features of the ferritin-mitochondrial interaction: i.e. mobilization of iron from ferritin followed by insertion of the iron into heme. The results support the concept of ferritin as a possible donor of iron to the mitochondria.

摘要

铁可以从铁蛋白中释放出来,并被分离的大鼠肝脏线粒体用于合成血红素。铁从铁蛋白的动员是通过铁蛋白与线粒体结合启动的,其方式与线粒体上铁蛋白的结合位点或受体相兼容。这种结合迅速完成,它不受温度影响,具有饱和性、可逆性,并且会被K+和Mg2+增强。铁蛋白结合位点的数量约为0.8 pmol/mg线粒体蛋白,亲和常数为6.4×10(6)M-1。结合动力学与铁蛋白-线粒体相互作用的功能特征密切相关:即铁从铁蛋白中动员出来,随后铁插入血红素中。这些结果支持了铁蛋白可能是线粒体铁供体的概念。

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