Melatonin receptors in purified cell nuclei of liver

D. Acuna-Castroviejo, M. I. Pablos, A. Menendez-Pelaez, R. J. Reiter

Research output: Contribution to journalArticlepeer-review

63 Scopus citations


Specific binding of [125I]iodomelatonin to homogenates from purified rat liver nuclei was characterized. The binding is rapid, reversible, saturable and of high affinity. Specific binding seems to be found in the nuclear protein fraction, since after precipitation of the proteins with trichloroacetic acid, the specific binding disappeared. The K(d) (180 ± 20 pM) and B(max) (9.1 ± 0.03 fmol/mg protein) values (mean ± S.E.M.) agree with the melatonin concentration in nuclei and may imply a physiological locus for melatonin action.

Original languageEnglish (US)
Pages (from-to)253-256
Number of pages4
JournalResearch Communications in Chemical Pathology and Pharmacology
Issue number2
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Toxicology
  • Pharmacology
  • Pharmacology, Toxicology and Pharmaceutics(all)


Dive into the research topics of 'Melatonin receptors in purified cell nuclei of liver'. Together they form a unique fingerprint.

Cite this