Solubilized active pituitary and ovarian gonadotropin-releasing hormone receptors retain binding properties for adenosine 3',5'-cyclic monophosphate derivatives.

The non-denaturing zwitterionic detergent, (3(3- cholamidopropyl )-dimethyl- ammonio )-1-propane sulfonate ( CHAPS ), has been used to solubilize membrane gonadotropin-releasing hormone (GnRH) receptors from rat ovaries. The solubilized receptors retain a high affinity (Ka = 1.85 +/- 0.3 nM-1), comparable to the affinity measured in membrane particles (Ka = 3.25 +/- 0.7 nM-1), and a preserved specificity for several analogs and fragments of GnRH. At millimolar concentrations, cyclic AMP derivatives inhibit [125I]-GnRH analog binding to both membrane particles and soluble receptors from pituitary and ovary. These results support the hypothesis that cyclic AMP may play the role of an extracellular messenger by interacting with the GnRH receptor itself.