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 S 20 o = 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.
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