Mack U, Powell L W, Halliday J W
J Biol Chem. 1983 Apr 25;258(8):4672-5.
A ferritin receptor has been detected on isolated rat hepatocytes and has been partially purified from rat liver using affinity chromatography. Isolated hepatocytes exhibit approximately 30,000 ferritin binding sites/cell with a binding association constant (Ka) of 1 x 10(8) mol-1 liter. A binding assay has been developed which utilizes a hepatic ferritin receptor coupled to a microparticulate support to facilitate separation of bound and free ligand. This method yielded a Ka of 3 x 10(8) mol-1 liter for the purified hepatic ferritin receptor. Binding of ferritin to the insolubilized receptor was partially inhibited by human lactoferrin but unaffected by 200-fold molar excess of bovine albumin, rat transferrin, or human asialoorosomucoid.
在分离出的大鼠肝细胞上已检测到铁蛋白受体，并且已使用亲和色谱法从大鼠肝脏中对其进行了部分纯化。分离出的肝细胞表现出大约30,000个铁蛋白结合位点/细胞，结合缔合常数（Ka）为1×10⁸ mol⁻¹升。已开发出一种结合测定法，该方法利用与微粒支持物偶联的肝铁蛋白受体来促进结合的和游离的配体的分离。该方法得到纯化的肝铁蛋白受体的Ka为3×10⁸ mol⁻¹升。铁蛋白与不溶性受体的结合被人乳铁蛋白部分抑制，但不受200倍摩尔过量的牛血清白蛋白、大鼠转铁蛋白或人去唾液酸糖蛋白的影响。
