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J. Biol. Chem., Vol. 262, Issue 18, 8668-8671, Jun, 1987

Isolation of the hemopexin receptor from human placenta

S Taketani, H Kohno, Y Naitoh and R Tokunaga

A hemopexin receptor detected in detergent-solubilized placental membranes was purified from the human placenta, using hemopexin- Sepharose affinity chromatography. The solubilized membranes exhibited binding sites of 2.77 pmol of hemopexin/mg of protein with a dissociation constant (Kd) of 6.6 X 10(-8) M. The purified receptor has a molecular weight of 80,000, determined on sodium dodecyl sulfate-gel electrophoresis. Immunoinhibition experiments using the antibody against the placental receptor revealed inhibition of binding of 125I- hemopexin to human leukemia K562 and HL 60 cells, thereby strongly supporting that the polypeptide isolated from the human placenta was the hemopexin receptor.
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