Isolation of human haemopexin by bioaffinity chromatography on haeme-sepharose.
A preparative procedure was developed for the isolation of human apohaemopexin from Cohn fraction IV or blood serum, based on bioaffinity chromatography on haeme-Sepharose. The isolation is carried out in the pH range 4-8; hence the possibility of degradation of the carbohydrate moiety of the glycoprotein in the acidic media used in other isolation procedures is decreased. Owing to the conditions of the separation and the good stability of the affinity support, the column can be used repeatedly for long periods without a significant loss of binding capacity. The reversibility of the conformational changes that haemopexin undergoes in acidic media was examined by hydrophobic chromatography. The original hydrophobic characteristics were restored only approximately 48 h after haemopexin had been brought into a neutral medium.
D002846:Chromatography, Affinity / Q000379:methods; D006466:Hemopexin / Q000302:isolation & purification*; D006801:Humans; D007122:Immunoelectrophoresis
D006466:Hemopexin