
pmid: 10903911
The chemokine receptor CXCR4 was solubilized from the human T-cell line CEM by using the detergent n-dodecyl-beta-maltoside (DDM) and cholesteryl hemisuccinate ester (CHS). Binding studies with (125)I-SDF-1alpha revealed a dissociation constant of 5.33 nM and a receptor density (B(max)) of 2.68 pmol/mg in CEM membranes at 4 degrees C. The affinity of solubilized CXCR4 for SDF-1alpha was identical to membrane-bound CXCR4. Binding of gp120 to solubilized CXCR4 was demonstrated by coprecipitation of gp120 with anti-CXCR4 antibodies.
Receptors, CXCR4, T-Lymphocytes, Cell Membrane, Detergents, HIV Envelope Protein gp120, Precipitin Tests, Chemokine CXCL12, Recombinant Proteins, Cell Line, Iodine Radioisotopes, Kinetics, Glucosides, HIV-1, Humans, Cholesterol Esters, Chemokines, CXC, Protein Binding
Receptors, CXCR4, T-Lymphocytes, Cell Membrane, Detergents, HIV Envelope Protein gp120, Precipitin Tests, Chemokine CXCL12, Recombinant Proteins, Cell Line, Iodine Radioisotopes, Kinetics, Glucosides, HIV-1, Humans, Cholesterol Esters, Chemokines, CXC, Protein Binding
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