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Isolation of the hemopexin receptor from human placenta.
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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Cited by 5 PubMed Central articles
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Identification and characterization of an iron-regulated hemopexin receptor in Haemophilus influenzae type b.
Wong JC, Holland J, Parsons T, Smith A, Williams P.
Infect Immun. 1994 Jan; 62(1):48-59.
[Infect Immun. 1994]
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Affinity, conservation, and surface exposure of hemopexin-binding proteins in Haemophilus influenzae.
Wong JC, Patel R, Kendall D, Whitby PW, Smith A, Holland J, Williams P.
Infect Immun. 1995 Jun; 63(6):2327-33.
[Infect Immun. 1995]
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Expression of haemopexin receptors by cultured human cytotrophoblast.
van Dijk HP, Kroos MJ, Starreveld JS, van Eijk HG, Tang SP, Song DX, Muller-Eberhard U.
Biochem J. 1995 May 1; 307 ( Pt 3):669-72.
[Biochem J. 1995]
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