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Production of platelet‐derived growth factor receptor (PDGFR‐β) in E. coli
Author(s) -
Rooney B.C.,
Hosang M.,
Hunziker W.
Publication year - 1994
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(94)80411-7
Subject(s) - receptor , recombinant dna , fusion protein , ligand (biochemistry) , platelet derived growth factor receptor , growth factor , growth factor receptor , extracellular , chemistry , microbiology and biotechnology , platelet derived growth factor , biochemistry , biology , gene
Portions of the extracellular domain of the platelet‐derived growth factor receptor β (PDGFR‐β) were expressed as fusion proteins with a hexa His tag in E. coli . Following purification by Ni chelate chromatography, the recombinant receptors were tested in cross‐competition studies with 125 I‐Iabelled PDGF‐AA and ‐BB. Although of lower affinity than the native receptor (IC 50 values of 10 −8 M) the recombinant molecules retained ligand binding specificity and neutralised the mitogenic effect of PDGF‐BB. These data indicate that the ligand binding region lies within the first four immunoglobulin‐like domains on PDGFR‐β. This E. coli expression system could be further used as a rapid and economical means to produce mutated receptors and map the ligand binding domain.