Halliday J W, Mack U, Powell L W
Br J Haematol. 1979 Aug;42(4):535-46. doi: 10.1111/j.1365-2141.1979.tb01166.x.
Significant differences were observed in the rate of disappearance from plasma of ferritins purified from rat serum and from different organs. Ferritin from all sources including purified serum ferritin was rapidly removed from plasma by the liver. No difference in biological half-life was observed between apoferritin prepared by ultracentrifugation of liver ferritin and whole liver ferritin and iron-loaded animals cleared injected serum ferritin from plasma at a comparable rate to normal rats. When amounts of 100 microgram of ferritin were injected into rats the half-life was significantly lengthened. The study confirmed the fact that ferritin iron and ferritin protein were removed from plasma at the same rate. No consistent effect of acidic or more basic isoferritin composition on biological half-life was apparent. After chromatography on concanavalin A-Sepharose 6B those ferritins which were predominantly bound to Con A-Sepharose had a half-life which was approximately twice that of ferritins which did not bind. It is concluded that the variation in plasma disappearance of ferritins of different tissue origin was explainable on the basis of carbohydrate content of the molecule.
从大鼠血清及不同器官纯化得到的铁蛋白,在血浆中的消失速率存在显著差异。包括纯化的血清铁蛋白在内,所有来源的铁蛋白都能被肝脏迅速从血浆中清除。通过超速离心肝脏铁蛋白制备的脱铁铁蛋白与全肝铁蛋白之间,以及铁负荷动物与正常大鼠清除注入血浆的血清铁蛋白的速率相当,未观察到生物半衰期的差异。当向大鼠注射100微克铁蛋白时,半衰期显著延长。该研究证实了铁蛋白铁和铁蛋白蛋白质从血浆中以相同速率清除这一事实。酸性或碱性更强的异铁蛋白组成对生物半衰期没有明显的一致影响。在伴刀豆球蛋白A-琼脂糖6B上进行层析后,那些主要与伴刀豆球蛋白A-琼脂糖结合的铁蛋白的半衰期约为未结合铁蛋白的两倍。得出的结论是,不同组织来源的铁蛋白在血浆中消失的差异可以根据分子的碳水化合物含量来解释。