Melatonin receptors in purified cell nuclei of liver

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

Melatonin receptors in purified cell nuclei of liver

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

Department of Cell Systems & Anatomy

Research output: Contribution to journal › Article › peer-review

65 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	253-256
Number of pages	4
Journal	Research Communications in Chemical Pathology and Pharmacology
Volume	82
Issue number	2
State	Published - 1993

ASJC Scopus subject areas

General Pharmacology, Toxicology and Pharmaceutics
Pathology and Forensic Medicine
Toxicology
Pharmacology

Cite this

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abstract = "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.",

author = "D. Acuna-Castroviejo and Pablos, \{M. I.\} and A. Menendez-Pelaez and Reiter, \{R. J.\}",

year = "1993",

language = "English (US)",

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journal = "Research Communications in Chemical Pathology and Pharmacology",

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T1 - Melatonin receptors in purified cell nuclei of liver

AU - Acuna-Castroviejo, D.

AU - Pablos, M. I.

AU - Menendez-Pelaez, A.

AU - Reiter, R. J.

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

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M3 - Article

C2 - 8303096

AN - SCOPUS:0027333179

SN - 0034-5164

VL - 82

SP - 253

EP - 256

JO - Research Communications in Chemical Pathology and Pharmacology

JF - Research Communications in Chemical Pathology and Pharmacology

IS - 2

ER -

Melatonin receptors in purified cell nuclei of liver

Abstract

ASJC Scopus subject areas

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