Solubilization of the Chemokine Receptor CXCR4

The chemokine receptor CXCR4 was solubilized from the human T-cell line CEM by using the detergent n-dodecyl-β-maltoside (DDM) and cholesteryl hemisuccinate ester (CHS). Binding studies with 125I-SDF-1α revealed a dissociation constant of 5.33 nM and a receptor density (Bmax) of 2.68 pmol/mg in CEM...

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Veröffentlicht in:	Biochemical and biophysical research communications 2000-07, Vol.274 (1), p.153-156
Hauptverfasser:	Staudinger, Robert, Bandres, Juan C.
Format:	Artikel
Sprache:	eng
Schlagworte:	AIDS/HIV Cell Line Cell Membrane - metabolism Chemokine CXCL12 chemokine receptor Chemokines, CXC - metabolism Cholesterol Esters - pharmacology coreceptor CXCR4 Detergents - pharmacology Glucosides - pharmacology gp120 HIV Envelope Protein gp120 - metabolism HIV-1 HIV-1 - metabolism Humans Iodine Radioisotopes - metabolism Kinetics Precipitin Tests Protein Binding Receptors, CXCR4 - isolation & purification Receptors, CXCR4 - metabolism Recombinant Proteins - metabolism SDF-1 solubilization T-Lymphocytes - metabolism
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Beschreibung
Zusammenfassung:	The chemokine receptor CXCR4 was solubilized from the human T-cell line CEM by using the detergent n-dodecyl-β-maltoside (DDM) and cholesteryl hemisuccinate ester (CHS). Binding studies with 125I-SDF-1α revealed a dissociation constant of 5.33 nM and a receptor density (Bmax) of 2.68 pmol/mg in CEM membranes at 4°C. The affinity of solubilized CXCR4 for SDF-1α was identical to membrane-bound CXCR4. Binding of gp120 to solubilized CXCR4 was demonstrated by coprecipitation of gp120 with anti-CXCR4 antibodies.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.2000.3109