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FEBS Lett. 1996 Oct 7;394(3):268-72.

Expression and pharmacological characterization of the human mu-opioid receptor in the methylotrophic yeast Pichia pastoris.

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1
Institut de Pharmacologie et de Biologie Structurale, CNRS-UPR 9062, Toulouse Cedex, France.

Abstract

The human mu-opioid receptor cDNA from which the 32 amino-terminal codons were substituted by the Saccharomyces cerevisiae alpha-mating factor signal sequence has been expressed in the methylotrophic yeast Pichia pastoris using the host promoter of the alcohol oxidase-1 gene. Cell membranes exhibited specific and saturable binding of the opioid antagonist [3H]diprenorphine (Kd = 0.2 nM and Bmax = 400 fmol/mg protein or 800 sites/cell). Competition studies with non-selective, and mu-, delta- and kappa-selective opioid agonists and antagonists revealed a typical mu-opioid receptor binding profile, suggesting proper folding of the protein in yeast membranes.

PMID:
8830656
[Indexed for MEDLINE]
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