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    J Biol Chem. 1987 Jun 25;262(18):8668-71.

    Isolation of the hemopexin receptor from human placenta.

    Taketani S, Kohno H, Naitoh Y, Tokunaga R.

    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.

    PMID: 3036819 [PubMed - indexed for MEDLINE]

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