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Solubilization of the chemokine receptor CXCR4
1Department of Pathology, Department of Neurology, Department of Medicine, New York University, School of Medicine, 423 East 23rd Street, New York, New York 10010, USA.
Biochemical and Biophysical Research Communications
|July 25, 2000
Abstract:
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.