Solubilization and characterization of opioid binding sites from frog (Rana esculenta) brain

J. Simon, M. Szucs, S. Benyhe

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

Active opioid receptors were solubilized from frog (Rana esculenta) brain membrane fractions by the use of 1% digitonin. It was found by kinetic as well as by equilibrium measurements that both the membrane and the solubilized fractions contain two binding sites. For the membrane preparations, K(D) values were 0.9 and 3.6 nM, and B(max) values were 293 and 734 fmol/mg protein. For the solubilized preparations, K(D) values were 0.4 and 2.6 nM, and B(max) values were 35 and 266 fmol/mg protein. The stereospecificity of the binding did not change during solubilization. Both the membrane-bound and the solubilized receptors showed weak binding of enkephalin and μ-specific drugs, suggesting that they are predominantly of the κ-type. The membrane-bound and the soluble receptors showed the same distribution of subtypes, i.e., 70% κ, 13% μ, and 17% δ for the membrane-bound and 71% κ, 17% μ, and 12% δ for the soluble receptors.

Original languageEnglish
Pages (from-to)957-963
Number of pages7
JournalJournal of Neurochemistry
Volume43
Issue number4
Publication statusPublished - 1984

Fingerprint

Rana esculenta
Anura
Opioid Analgesics
Brain
Binding Sites
Membranes
Digitonin
Enkephalins
Opioid Receptors
Proteins
Kinetics
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Solubilization and characterization of opioid binding sites from frog (Rana esculenta) brain. / Simon, J.; Szucs, M.; Benyhe, S.

In: Journal of Neurochemistry, Vol. 43, No. 4, 1984, p. 957-963.

Research output: Contribution to journalArticle

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N2 - Active opioid receptors were solubilized from frog (Rana esculenta) brain membrane fractions by the use of 1% digitonin. It was found by kinetic as well as by equilibrium measurements that both the membrane and the solubilized fractions contain two binding sites. For the membrane preparations, K(D) values were 0.9 and 3.6 nM, and B(max) values were 293 and 734 fmol/mg protein. For the solubilized preparations, K(D) values were 0.4 and 2.6 nM, and B(max) values were 35 and 266 fmol/mg protein. The stereospecificity of the binding did not change during solubilization. Both the membrane-bound and the solubilized receptors showed weak binding of enkephalin and μ-specific drugs, suggesting that they are predominantly of the κ-type. The membrane-bound and the soluble receptors showed the same distribution of subtypes, i.e., 70% κ, 13% μ, and 17% δ for the membrane-bound and 71% κ, 17% μ, and 12% δ for the soluble receptors.

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