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Isolation and reconstitution of the N ‐formylpeptide receptor from HL‐60 derived neutrophils
Author(s) -
Hoyle Peter C.,
Freer Richard J.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80142-8
Subject(s) - receptor , affinity chromatography , chemistry , selectivity , formyl peptide receptor , membrane , phosphatidylcholine , biochemistry , microbiology and biotechnology , biophysics , biology , chemotaxis , phospholipid , enzyme , catalysis
A multifunctional receptor for N ‐formylpeptides exists on the membranes of neutrophils. This receptor has now been isolated from neutrophils derived from HL‐60 promyelocytic leukemia cells. After solubilization by Nonidet‐P40 and purification by affinity chromatography and HPLC the isolated receptor was reconstituted into egg phosphatidylcholine vesicles by SM‐2 Bio‐Bead removal of the Nonidet‐P40. Analysis of the affinity and selectivity of the receptor was done by direct binding of two high‐affinity ligands, formyl‐Met‐Leu‐[ 3 H]Phe‐OH and formyl‐Nle‐Leu‐Phe[ 3 H]Tyr‐OH. The data suggest that the receptor can be isolated and reconstituted without apparent alteration of its binding affinity and selectivity, and that there appear to be no co‐factors or subunits upon which these binding characteristics are dependent.