Vretblad P, Hjorth R
Biochem J. 1977 Dec 1;167(3):759-64. doi: 10.1042/bj1670759.
Haemopexin was prepared in 37% yield from normal human serum by a simple procedure involving fractional poly(ethylene glycol) precipitation and subsequent chromatography on DEAE-Sepharose CL-6B. One peak from the ion exchanger consisted of only haemopexin and transferrin. These proteins were separated by chromatography on wheat-germ lectin-Sepharose 6MB. Haemopexin was selectively bound and was subsequently desorbed by N-acetyl-D-glucosamine. No impurities could be detected in the final preparation by immunoelectrophoresis or by immunodiffusion against a range of antisera. The protein gave two partially separated bands in polyacrylamide-gradient-gel electrophoresis, corresponding to apohaemopexin and haem-haemopexin complex.
通过一种简单的方法从正常人血清中制备血红素结合蛋白，产率为37%，该方法包括聚（乙二醇）分级沉淀以及随后在DEAE-琼脂糖CL-6B上进行色谱分离。离子交换柱上的一个峰仅由血红素结合蛋白和转铁蛋白组成。通过在麦胚凝集素-琼脂糖6MB上进行色谱分离将这些蛋白质分开。血红素结合蛋白被选择性结合，随后用N-乙酰-D-葡萄糖胺解吸。通过免疫电泳或针对一系列抗血清的免疫扩散在最终制剂中未检测到杂质。该蛋白质在聚丙烯酰胺梯度凝胶电泳中给出两条部分分离的条带，对应于脱辅基血红素结合蛋白和血红素-血红素结合蛋白复合物。
