Conrad M E, Umbreit J N, Moore E G, Peterson R D, Jones M B
Department of Medicine, University of South Alabama, Mobile 36688.
J Biol Chem. 1990 Mar 25;265(9):5273-9.
An iron binding protein with an approximate molecular mass of 56,000 daltons was purified to homogeneity from homogenates of rat duodenal mucosa. The protein was biochemically and immunologically distinct from transferrin and ferritin and competitively bound cobalt, copper, zinc, and lead. Each molecule bound one molecule of iron with a Kd of 9 X 10(-5). Dissociation of iron and the protein was accelerated at acid pH. Using an immunogold method, the protein was identified in the apical cytoplasm of proximal small intestinal cells and was not observed elsewhere in the intestinal mucosa and in other body organs. It was named mobilferrin from its city of origin and to differentiate it from other previously identified iron binding proteins.
从大鼠十二指肠黏膜匀浆中纯化出一种分子量约为56,000道尔顿的铁结合蛋白，使其达到同质状态。该蛋白在生化和免疫方面与转铁蛋白和铁蛋白不同，能竞争性结合钴、铜、锌和铅。每个分子结合一个铁分子，解离常数Kd为9×10⁻⁵。在酸性pH条件下，铁与该蛋白的解离加速。采用免疫金法，在近端小肠细胞的顶端细胞质中鉴定出该蛋白，在肠黏膜的其他部位及其他身体器官中未观察到。因其来源地而命名为可动铁蛋白，以区别于其他先前鉴定的铁结合蛋白。
