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. 1977 Dec 1;167(3):759-64.
doi: 10.1042/bj1670759.

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

P Vretblad, R Hjorth

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

P Vretblad et al. Biochem J. .

Abstract

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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