人脱铁转铁蛋白与网织红细胞的相互作用。
Interaction of human diferric transferrin with reticulocytes.
作者信息
Huebers H, Csiba E, Josephson B, Huebers E, Finch C
出版信息
Proc Natl Acad Sci U S A. 1981 Jan;78(1):621-5. doi: 10.1073/pnas.78.1.621.
Abstract
Methods have been devised for preparing human transferrin with a different isotope of iron selectively labeling each of the two iron binding sites and for determining the distribution of radioiron among transferrin molecules. When diferric human transferrin was exposed to human or animal reticulocytes, there was an equal contribution of radioiron from the acid-stable and acid-labile sites. In this delivery, both atoms of iron were removed simultaneously from the diferric transferrin molecule, converting it to apotransferrin. At similar iron concentrations the amount of iron delivered by diferric transferrin was twice that delivered by monoferric transferrin.
摘要
已设计出一些方法，用于制备在两个铁结合位点分别选择性标记不同铁同位素的人转铁蛋白，以及用于测定放射性铁在转铁蛋白分子中的分布。当二价铁人转铁蛋白与人类或动物网织红细胞接触时，酸稳定位点和酸不稳定位点对放射性铁的贡献相等。在这种传递过程中，二价铁转铁蛋白分子中的两个铁原子同时被去除，将其转化为脱铁转铁蛋白。在相似的铁浓度下，二价铁转铁蛋白传递的铁量是一价铁转铁蛋白传递铁量的两倍。
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