Grasso J A, Hillis T J, Mooney-Frank J A
Biochim Biophys Acta. 1984 Feb 14;797(2):247-55. doi: 10.1016/0304-4165(84)90128-4.
Pulse-chase analysis of newt (Triturus cristatus) erythroblasts has shown that ferritin is not a primary source of iron for heme synthesis. During chase incubation with and without non-radioactive plasma iron in the medium, no transfer of 59Fe from ferritin to hemoglobin was detected although the integrity of heme synthesis was maintained. In puromycin-inhibited cells where iron uptake was drastically curtailed, heme synthesis continued to occur, though at reduced levels; incorporation of 59Fe from the plasma appeared initially in heme and hemoglobin without any prior labelling of ferritin. These results indicate that ferritin is neither an obligatory iron intermediate in heme synthesis nor a cytosolic transport molecule involved in mobilization of iron from the transferrin-receptor complex. The most likely role for erythroid ferritin is storage of excess iron.
对蝾螈（Triturus cristatus）成红细胞进行的脉冲追踪分析表明，铁蛋白并非血红素合成中铁的主要来源。在有和没有非放射性血浆铁的培养基中进行追踪孵育期间，尽管血红素合成的完整性得以维持，但未检测到59Fe从铁蛋白转移至血红蛋白。在嘌呤霉素抑制的细胞中，铁摄取大幅减少，血红素合成仍继续发生，尽管水平有所降低；来自血浆的59Fe最初掺入血红素和血红蛋白中，而铁蛋白未事先标记。这些结果表明，铁蛋白既不是血红素合成中必不可少的铁中间体，也不是参与从转铁蛋白-受体复合物中动员铁的胞质转运分子。红细胞铁蛋白最可能的作用是储存过量的铁。
