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.
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Research Article| December 01 1977
The use of wheat-germ lectin-Sepharose for the purification of human haemopexin
Biochem J (1977) 167 (3): 759–764.
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P Vretblad, R Hjorth; The use of wheat-germ lectin-Sepharose for the purification of human haemopexin. Biochem J 1 December 1977; 167 (3): 759–764. doi: https://doi.org/10.1042/bj1670759
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