DETECTION OF 4 MOLECULAR-FORMS OF HUMAN TRANSFERRIN DURING IRON-BINDING PROCESS
DETECTION OF 4 MOLECULAR-FORMS OF HUMAN TRANSFERRIN DURING IRON-BINDING PROCESS
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DOI：
10.1016/0005-2795(76)90270-1
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发表时间：
1976-01-01
期刊：
影响因子：
--
通讯作者：
SEAL, US
中科院分区：
文献类型：
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作者：
MAKEY, DG;SEAL, US
通过在含有6 M尿素和Tris/硼酸盐/EDTA（pH 8.4）缓冲液的培养基中电泳，将人转铁蛋白分离成4种分子形式。这些形式的分离与转铁蛋白结合的Fe的量直接相关：不含Fe的转铁蛋白、仅与转铁蛋白的位点A结合的Fe、仅与转铁蛋白的位点B结合的Fe和与转铁蛋白的两个Fe结合位点结合的Fe。电泳分离人转铁蛋白为4种分子形式的分子基础是复杂的，目前还没有完全确定。这种分离似乎与在这项工作中观察到的2种现象和其他研究人员：铁结合转铁蛋白和转铁蛋白分子中氨基酸的不对称分布时蛋白质稳定性的增加有关。观察到的现象在进一步评估转铁蛋白参与的物理化学和生理过程中具有潜在的用途。
Human transferrin was separated into 4 molecular forms by electrophoresis in a medium containing 6 M urea and a Tris/borate/EDTA, pH 8.4, buffer. The separation of these forms correlates directly with the amount of Fe bound by the transferrin: Fe free transferrin, Fe bound only to site A of transferrin, Fe bound only to site B of transferrin and Fe bound to both Fe binding sites of transferrin. The molecular basis for the electrophoretic separation of human transferrin into 4 molecular forms is complex and incompletely defined at this time. This separation appears to be related to 2 phenomena observed in this work and by other investigators: the increase in protein stability as Fe is bound to transferrin and the assymetrical distribution of amino acids in the transferrin molecule. The observed phenomenon has potential use in further evaluation of both the physicochemical and physiological processes in which transferrin participates.