Adams P C, Powell L W, Halliday J W
Department of Medicine, University of Queensland, Royal Brisbane Hospital, Australia.
Hepatology. 1988 Jul-Aug;8(4):719-21. doi: 10.1002/hep.1840080402.
A human hepatic ferritin receptor has been isolated from human liver and has been purified using affinity chromatography. An affinity constant of 6.0 x 10(8) moles-1 liter was determined for the ferritin receptor. The molecular weight was estimated to be approximately 53,000 by gel electrophoresis. Binding of ferritin to the receptor coupled to a microparticulate support was specific for human liver ferritin with no binding of rat or porcine ferritin. Binding was unaffected by a 100-fold excess of human transferrin, human asialoorosomucoid and bovine albumin. After treatment of the receptor protein with trypsin, binding was not detected. The human hepatic ferritin receptor may play an important role in the uptake of iron into the hepatocyte in physiological and pathological conditions.
一种人肝铁蛋白受体已从人肝脏中分离出来，并通过亲和色谱法进行了纯化。测定该铁蛋白受体的亲和常数为6.0×10⁸摩尔⁻¹升。通过凝胶电泳估计其分子量约为53,000。与微粒支持物偶联的铁蛋白与受体的结合对人肝铁蛋白具有特异性，大鼠或猪铁蛋白无结合。100倍过量的人转铁蛋白、人去唾液酸糖蛋白和牛血清白蛋白不影响结合。用胰蛋白酶处理受体蛋白后，未检测到结合。人肝铁蛋白受体在生理和病理条件下铁进入肝细胞的过程中可能起重要作用。
