The use of wheat-germ lectin-Sepharose for the purification of human haemopexin

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Abstract
Hemopexin 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 hemopexin and transferrin. These proteins were separated by chromatography on wheat-germ lectin-Sepharose 6MB. Hemopexin was selectively bound and was subsequently desorbed by N-acetyl-D-glycosamine. No impurities could be detected in the final preparation by immunoelectrophoresis or by immunodiffusion against a range of antisera. The protein gave 2 partially separated bands in polyacrylamide-gradient-gel electrophoresis, corresponding to apohemopexin and heme-hemopexin complex.