通过等电聚焦分析转铁蛋白的铁结合位点。

Analysis of the iron-binding sites of transferrin by isoelectric focussing.

van Eijk H G, van Noort W L, Kroos M J, van der Heul C

J Clin Chem Clin Biochem. 1978 Oct;16(10):557-60. doi: 10.1515/cclm.1978.16.10.557.

Abstract

Human transferrin was labelled with ferric nitrilotriacetate (FeNTA) at one of its two metal binding sites by variation of the pH. 2. Four transferrin forms, transferrin, transferrin(Fe) (A-site), transferrin(Fe) (B-site) and transferrin(2Fe) could be separated on flat bed gels by isoelectric focussing. 3. Incubation time, temperature and medium play an important role in the specificity of the binding of Fe. In NTA-pH-buffer, at 0.5 Fe-saturation, the A-site was preferentially labelled at pH 7--8, the B-site at a pH 8--9. 4. Under physiological conditions iron from the B-site has the tendency to move to the A-site.

摘要

通过改变pH值，在人转铁蛋白两个金属结合位点之一用次氮基三乙酸铁（FeNTA）进行标记。2. 四种转铁蛋白形式，即转铁蛋白、转铁蛋白（铁）（A位点）、转铁蛋白（铁）（B位点）和转铁蛋白（2铁），可通过等电聚焦在平板凝胶上分离。3. 孵育时间、温度和介质在铁结合的特异性中起重要作用。在NTA - pH缓冲液中，在0.5铁饱和度下，A位点在pH 7 - 8时优先被标记，B位点在pH 8 - 9时被标记。4. 在生理条件下，来自B位点的铁有向A位点移动的趋势。