Ulvik R, Prante P H, Koller M E, Romslo I
Scand J Clin Lab Invest. 1976 Oct;36(6):539-46. doi: 10.3109/00365517609054476.
Isolated rat liver mitochondria accumulate iron from the suspending medium when [59Fe]transferrin is used as a model compound. The accumulation proceeds by two different mechanisms, i.e. by an energy-independent and an energy-dependent (uncoupler sensitive) mechanism, which have different time, pH, and temperature dependencies. The energy-dependent accumulation, which is inhibited by ruthenium red and sulphydryl reagents, reaches a saturation level of approx. 30 pmoles iron/mg protein during 30 min incubation. The energy-independent accumulation of iron-transferrin reveals no saturation kinetics, it is inhibited neither by ruthenium red nor by N-ethylmaleimide, and it proceeds linearly for at least 90 min. With [125I]transferrin as a model compound, quantitatively the energy-independent accumulation is as reported for [59Fe]transferrin. There is, however, no energy-dependent accumulation of [125I]transferrin. The results indicate that the energy-dependent accumulation of [59Fe]transferrin represents a process by which mitochondria accumulate iron from transferrin.
当使用[59Fe]转铁蛋白作为模型化合物时，分离的大鼠肝线粒体可从悬浮培养基中积累铁。积累过程通过两种不同机制进行，即通过能量非依赖机制和能量依赖（解偶联剂敏感）机制，这两种机制具有不同的时间、pH和温度依赖性。能量依赖型积累受到钌红和巯基试剂的抑制，在30分钟孵育期间达到约30皮摩尔铁/毫克蛋白质的饱和水平。铁-转铁蛋白的能量非依赖型积累未显示饱和动力学，既不受钌红也不受N-乙基马来酰亚胺的抑制，并且至少持续90分钟呈线性进行。以[125I]转铁蛋白作为模型化合物，在定量方面，能量非依赖型积累与[59Fe]转铁蛋白的报道一致。然而，[125I]转铁蛋白不存在能量依赖型积累。结果表明，[59Fe]转铁蛋白的能量依赖型积累代表线粒体从转铁蛋白中积累铁的过程。
