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Localization and quantification of high‐affinity melatonin binding sites in Rana pipiens retina
Author(s) -
Wiechmann Allan F.,
WirsigWiechmann Celeste R.
Publication year - 1991
Publication title -
journal of pineal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.881
H-Index - 131
eISSN - 1600-079X
pISSN - 0742-3098
DOI - 10.1111/j.1600-079x.1991.tb00812.x
Subject(s) - melatonin , rana , melatonin receptor , dissociation constant , retina , medicine , endocrinology , biology , radioligand , grenouille , receptor , inner plexiform layer , population , binding site , retinal , outer plexiform layer , biophysics , chemistry , biochemistry , salientia , neuroscience , xenopus , environmental health , gene
Melatonin binding was localized to the inner plexiform layer (IPL) of the frog retina by in vitro autoradiography, using 2‐ 125 I‐melatonin as the radioligand. Radioreceptor binding assays of frog retinal homogehate demonstrated saturable melatonin binding. Scatchard analysis revealed a single population of binding sites with an apparent dissociation constant (K d ) of 125 pM, with a B max of 0.138 fmoles/mg of protein. These results suggest that high‐affinity melatonin binding sites are present in the IPL of the frog retina, which may reflect the presence of melatonin receptors in this synaptic layer.

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