趋化因子受体CXCR4的增溶作用。

Solubilization of the chemokine receptor CXCR4.

作者信息

Staudinger R, Bandres J C

机构信息

Department of Pathology, Department of Neurology, Department of Medicine, New York University, School of Medicine, 423 East 23rd Street, New York, New York 10010, USA.

出版信息

Biochem Biophys Res Commun. 2000 Jul 21;274(1):153-6. doi: 10.1006/bbrc.2000.3109.

DOI:10.1006/bbrc.2000.3109

PMID:10903911

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.

摘要

通过使用去污剂正十二烷基-β-麦芽糖苷（DDM）和胆固醇半琥珀酸酯（CHS），从人T细胞系CEM中溶解趋化因子受体CXCR4。在4℃下，用（125）I-SDF-1α进行的结合研究显示，CEM细胞膜中解离常数为5.33 nM，受体密度（Bmax）为2.68 pmol/mg。溶解的CXCR4对SDF-1α的亲和力与膜结合的CXCR4相同。通过抗CXCR4抗体与gp120共沉淀证明了gp120与溶解的CXCR4的结合。