Abstract
Ligand binding properties were investigated in recombinant human α 2C2-adrenoceptors expressed in three different host systems: Shionogi S115 mouse mammary tumour cells, Spodoptera frugiperda Sf9 insect cells and Saccharomyces cerevisae yeast cells. The expected 43 kDa α 2C2 protein was visualized with immunoblotting using a polyclonal α 2C2-receptor antibody. [ 3H]Rauwolscine binding in cell homogenates or membranes ( B max 3–11 pmol/mg protein; K d approximately 5.5 nM) was inhibited by prazosin, oxymetazoline, RX821002, chlorpromazine and (−)-noradrenaline with and without the GTP-analogue Gpp(NH)p with similar K i values in the different host systems. This indicates that α 2C2-adrenoceptors retain their binding characteristics irrespective of the host environment.
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