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In Vitro Interaction between Ceruloplasmin and Human Serum Transferrin

机译:铜蓝蛋白和人类血清转铁蛋白之间的体外相互作用

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摘要

The thermodynamics of the interactions of serum apotransferrin (T) and holotransferrin (TFe2) with ceruloplasmin (Cp), as well as those of human lactoferrin (Lf), were assessed by fluorescence emission spectroscopy. Cp interacts with two Lf molecules. The first interaction depends on pH and whereas the second does not. Dissociation constants were as follows: K-11Lf = 1.5 +/- 0.2 mu M, and K-12Lf = 11 +/- 2 mu M. Two slightly different interactions of T or TFe2, with Cp are detected for the first time. They are both independent of pH and it and occur with I stoichiometry: K-1T = 19 +/- 7 mu M, and K-1TFe2 = 12 +/- 4 mu M. These results can improve our understanding of the probable process of the transfer of iron from Cp to T in iron and copper transport and homeostasis.
机译:通过荧光发射光谱法评估了血清载脂蛋白(T)和全运铁蛋白(TFe2)与铜蓝蛋白(Cp)以及人乳铁蛋白(Lf)的相互作用的热力学。 Cp与两个Lf分子相互作用。第一次相互作用取决于pH,而第二次则不依赖于pH。解离常数如下:K-11Lf = 1.5 +/- 0.2μM,K-12Lf = 11 +/- 2μM。首次检测到T或TFe2与Cp的两种略有不同的相互作用。它们都与pH无关,并且与pH呈化学计量关系:K-1T = 19 +/- 7μM,K-1TFe2 = 12 +/- 4μM。这些结果可以帮助我们更好地理解铁和铜的运输和体内稳态中铁从Cp向T的转移。

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