Characterization of 2-[125I]iodomelatonin-binding sites in quail testes at mid-light and mid-dark
| Autor: | Gregory M. Brown, Zheng Pin Wang, Shiu Fun Pang, Kimberly M. Cheng, Celia Sook-Fun Pang |
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| Rok vydání: | 1992 |
| Předmět: |
Male
endocrine system medicine.medical_specialty Light Receptors Melatonin Coturnix Testicle Melatonin receptor Melatonin Internal medicine biology.animal Testis medicine Animals Circadian rhythm Binding site biology General Neuroscience Diurnal temperature variation Darkness Quail Receptors Neurotransmitter Dissociation constant Kinetics Endocrinology medicine.anatomical_structure medicine.drug |
| Zdroj: | Neuroscience Letters. 146:195-198 |
| ISSN: | 0304-3940 |
| DOI: | 10.1016/0304-3940(92)90076-j |
| Popis: | The binding and pharmacological characteristics of 2-[ 125 I]iodomelatonin binding sites in testis membrane preparations of quails were examined. Scatchard analyses yielded an equilibrium dissociation constant ( K d ) of 46.6 ± 8.6 pmol/l and maximum binding capacity ( B max ) of 2.77 ± 0.20 fmol/mg protein for the gonadal 2-[ 125 I]iodomelatonin binding sites. Except for melatonin, 6-chloromelatonin, 2-iodomelatonin and N -acetylsero-tonin, 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-[ 125 I]iodomelatonin binding sites in quails. Results of the present study suggest possible direct gonadal action by pineal melatonin in birds. |
| Databáze: | OpenAIRE |
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