Detergent solubilisation of the rabbit neutrophil receptor for chemotactic formyl peptides
- 1 October 1983
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 135 (3), 515-518
- https://doi.org/10.1111/j.1432-1033.1983.tb07682.x
Abstract
Digitonin was found to be the only detergent (out of 24 tested) capable of solubilizing the chemotactic formyl peptide receptor from rabbit neutrophil membranes in a form which retained its [3H]fMet-Leu-Phe binding activity. The solubilized material retained many of the characteristics of the membrane-bound receptor. [3H]fMet-Leu-Phe binding to the digitonin extract was measured at 4.degree. C using an equilibrium dialysis assay. Binding was saturable and of high affinity (Kd = 3.5 .+-. 0.7 nM). The potencies of a series of synthetic peptides as inhibitors of [3H]fMet-Leu-Phe binding to the soluble receptor showed the same rank order as for inhibition of the membrane-bound receptor. In addition, binding to both preparations was SH dependent showing a parallel inhibition by p-chloromercuribenzene sulphonate which could be partially reversed be subsequent incubation with dithiothreitol.This publication has 17 references indexed in Scilit:
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