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首页> 外文期刊>Biochemistry >Interaction kinetics of tetramethylrhodamine transferrin with human transferrin receptor studied by fluorescence correlation spectroscopy.
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Interaction kinetics of tetramethylrhodamine transferrin with human transferrin receptor studied by fluorescence correlation spectroscopy.

机译：荧光相关光谱研究了四甲基若丹明转铁蛋白与人转铁蛋白受体的相互作用动力学。

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摘要

We applied fluorescence correlation spectroscopy (FCS) to characterize the interaction dynamics of fluorescence-labeled transferrin with transferrin receptor (hTfR) associates isolated from human placenta. The dissociation constant for the equilibrium binding of TMR-labeled ferri-transferrin to hTfR in detergent free solution was determined to be 7 +/- 3 nM. Binding curves were compatible with equal and independent binding sites present on the hTfR associates. Under pseudo-first-order conditions, with respect to transferrin, complex formation is monophasic. From these curves, association and dissociation rate constants for a reversible bimolecular binding reaction were determined, with (1.1 +/- 0.1) x 10(4) M-1 s-1 for the former and (6 +/- 4) x 10(-)4 s-1 for the latter. In dissociation exchange experiments, biphasic curves and concentration-independent reciprocal relaxation times were determined. From isothermal titration calorimetry experiments, we obtained an enthalpy change of -44.4 kJ/mol associated with the reaction. We thus conclude that the reaction is mainly enthalpy driven.
机译：我们应用荧光相关光谱法（FCS）来表征荧光标记的转铁蛋白与从人胎盘分离的转铁蛋白受体（hTfR）缔合体的相互作用动力学。在无洗涤剂的溶液中，TMR标记的铁转铁蛋白与hTfR的平衡结合的解离常数确定为7 +/- 3 nM。结合曲线与hTfR缔合体上存在的相等和独立的结合位点相容。在伪一阶条件下，就转铁蛋白而言，复合物的形成是单相的。从这些曲线，确定可逆双分子结合反应的缔合和解离速率常数，前者为（1.1 +/- 0.1）x 10（4）M-1 s-1，前者为（6 +/- 4）x 10后者为（-）4 s-1。在解离交换实验中，确定了双相曲线和浓度独立的倒数弛豫时间。从等温滴定热法实验中，我们得到与反应相关的-44.4 kJ / mol的焓变。因此，我们得出结论，该反应主要是焓驱动的。

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