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Article: 2[125I]Iodomelatonin binding sites in spleens of guinea pigs

Title2[125I]Iodomelatonin binding sites in spleens of guinea pigs
Authors
Issue Date1992
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/lifescie
Citation
Life Sciences, 1992, v. 50 n. 22, p. 1719-1726 How to Cite?
Abstract2-[125I]Iodomelatonin was found to bind specifically to the membrane preparations of the spleens of guinea pigs with high affinity. The binding was rapid, stable, saturable and reversible. Scatchard analysis of the binding assays revealed an equilibrium dissociation constant (Kd) of 49.8 ± 4.12 pmol/l and binding site density (Bmax) of 0.69 ± 0.082 fmol/mg protein at mid-light (n = 10). There was no significant change in the Kd (41.8 ± 3.16 pmol/l) or the Bmax (0.58 ± 0.070 fmol/mg protein) at mid-dark (n = 10). Kinetic analysis showed a Kd of 23.13 ± 4.81 pmol/l (mean ± SE, n = 4), in agreement to that derived from the saturation studies. The 2-[125I]iodomelatonin binding sites have the following order of potency: 2-iodomelatonin > melatonin > 6-chloromelatonin >> N-acetylserotonin, 6-hydroxymelatonin > 5-methoxytryptamine, 5 methoxytryptophol > serotonin, 5-methoxyindole-3-acetic acid > 5-hydroxytryptophol, 3-acetylindole, 1-acetylindole-3-carboxyaldehyde, L-tryptophan > tryptamine, 5-hydroxyindole-3-acetic acid. Differential centrifugation studies showed that the binding sites are localized mainly in the nuclear fraction (65.5%), the rest are distributed in the microsomal fraction (17.4%), mitochondrial fraction (14.7%) and cytosolic fraction (0.3%). The demonstration of 2-[125I]iodomelatonin binding sites in the spleen suggests the presence of melatonin receptors and a direct mechanism of action of melatonin on the immune system.
Persistent Identifierhttp://hdl.handle.net/10722/171568
ISSN
2015 Impact Factor: 2.685
2015 SCImago Journal Rankings: 1.056
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorPoon, AMSen_US
dc.contributor.authorPang, SFen_US
dc.date.accessioned2012-10-30T06:15:43Z-
dc.date.available2012-10-30T06:15:43Z-
dc.date.issued1992en_US
dc.identifier.citationLife Sciences, 1992, v. 50 n. 22, p. 1719-1726en_US
dc.identifier.issn0024-3205en_US
dc.identifier.urihttp://hdl.handle.net/10722/171568-
dc.description.abstract2-[125I]Iodomelatonin was found to bind specifically to the membrane preparations of the spleens of guinea pigs with high affinity. The binding was rapid, stable, saturable and reversible. Scatchard analysis of the binding assays revealed an equilibrium dissociation constant (Kd) of 49.8 ± 4.12 pmol/l and binding site density (Bmax) of 0.69 ± 0.082 fmol/mg protein at mid-light (n = 10). There was no significant change in the Kd (41.8 ± 3.16 pmol/l) or the Bmax (0.58 ± 0.070 fmol/mg protein) at mid-dark (n = 10). Kinetic analysis showed a Kd of 23.13 ± 4.81 pmol/l (mean ± SE, n = 4), in agreement to that derived from the saturation studies. The 2-[125I]iodomelatonin binding sites have the following order of potency: 2-iodomelatonin > melatonin > 6-chloromelatonin >> N-acetylserotonin, 6-hydroxymelatonin > 5-methoxytryptamine, 5 methoxytryptophol > serotonin, 5-methoxyindole-3-acetic acid > 5-hydroxytryptophol, 3-acetylindole, 1-acetylindole-3-carboxyaldehyde, L-tryptophan > tryptamine, 5-hydroxyindole-3-acetic acid. Differential centrifugation studies showed that the binding sites are localized mainly in the nuclear fraction (65.5%), the rest are distributed in the microsomal fraction (17.4%), mitochondrial fraction (14.7%) and cytosolic fraction (0.3%). The demonstration of 2-[125I]iodomelatonin binding sites in the spleen suggests the presence of melatonin receptors and a direct mechanism of action of melatonin on the immune system.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/lifescieen_US
dc.relation.ispartofLife Sciencesen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCell Nucleus - Metabolismen_US
dc.subject.meshCircadian Rhythmen_US
dc.subject.meshCytosol - Metabolismen_US
dc.subject.meshFemaleen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshIodine Radioisotopesen_US
dc.subject.meshKineticsen_US
dc.subject.meshMelatonin - Analogs & Derivatives - Metabolismen_US
dc.subject.meshMicrosomes - Metabolismen_US
dc.subject.meshMitochondria - Metabolismen_US
dc.subject.meshReceptors, Melatoninen_US
dc.subject.meshReceptors, Neurotransmitter - Metabolismen_US
dc.subject.meshSpleen - Metabolismen_US
dc.title2[125I]Iodomelatonin binding sites in spleens of guinea pigsen_US
dc.typeArticleen_US
dc.identifier.emailPoon, AMS:amspoon@hkucc.hku.hken_US
dc.identifier.authorityPoon, AMS=rp00354en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0024-3205(92)90427-Qen_US
dc.identifier.pmid1316983-
dc.identifier.scopuseid_2-s2.0-0026611419en_US
dc.identifier.volume50en_US
dc.identifier.issue22en_US
dc.identifier.spage1719en_US
dc.identifier.epage1726en_US
dc.identifier.isiWOS:A1992HQ39700008-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridPoon, AMS=7103068868en_US
dc.identifier.scopusauthoridPang, SF=7402528719en_US

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