Characterization of 2-[125I]iodomelatonin-binding sites in quail testes at mid-light and mid-dark

The binding and pharmacological characteristics of 2-[125I]iodomelatonin binding sites in testis membrane preparations of quails were examined. Scatchard analyses yielded an equilibrium dissociation constant (Kd) of 46.6 +/- 8.6 pmol/l and maximum binding capacity (Bmax) of 2.77 +/- 0.20 fmol/mg protein for the gonadal 2-[125I]iodomelatonin binding sites. Except for melatonin, 6-chloromelatonin, 2-iodomelatonin and N-acetylserotonin, all compounds tested elicited no significant inhibition of radioligand binding. Significant diurnal variations were detected in serum melatonin levels of 24-week-old quails while no diurnal difference was detected in the affinities or densities of the gonadal 2-[125I]iodomelatonin binding sites in quails. Results of the present study suggest possible direct gonadal action by pineal melatonin in birds.