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Isolation and study of human hemopexin (author's transl)
Authors:A Hayem-Lévy  R Havez
Affiliation:Unité de Recherches de l''INSERM sur la Biochimie des Protéines, Faculté de Médecine, Place de Verdun, 51)045 Lille Cedex France
Abstract:
Human hemopexin is a β-glycoprotein which binds hemin, myoglobin and cytochrome c.The isolation method here described involves the use of precipitation with Rivanol, followed by ammonium sulfate precipitation. The final step is recycling chromatography on Sephadex G-100. Hemopexin is obtained in a pure state after four cycles. The sedimentation constant is S20o= 3.9. The N-terminal amino acid is threonin, and the C-terminal amino acid is histidin. Hemopexin binds hemin through two residues of histidin.
Keywords:
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