Characterization of solubilized opiate receptors from human placenta

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

A solubilized opiate receptor from human pla-cental membranes binds [3H]etorphine saturably, reversibly, and stereospecifically. The binding activity is shown to be truly soluble because it migrates between two soluble proteins on Se-pharose CL-6B. The solubilized macromolecular complex behaves as a molecule with an apparent Stokes radius of 70 A and contains a protein as an essential constituent. The solubilized receptors bind [3H]ethylketocyclazocine with high affinity in a saturable and stereospecific manner. Naloxone inhibits [3H]etorphine and [3H]ethylketocyclazocine binding to the solubilized receptor. Sodium inhibits [3H]etorphine but not [3H]naloxone binding. These observations indicate that the solubilized receptor from human placental membranes is active and retains properties of membrane-bound receptors.

Original languageEnglish (US)
Pages (from-to)35-47
Number of pages13
JournalMolecular Membrane Biology
Volume5
Issue number1
DOIs
StatePublished - 1983
Externally publishedYes

Fingerprint

Etorphine
Opioid Receptors
Ethylketocyclazocine
Placenta
Naloxone
Membranes
Macromolecular Substances
Proteins
Sodium
Molecules

Keywords

  • Human placenta
  • Solubilized opiate receptors

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Cite this

Characterization of solubilized opiate receptors from human placenta. / Ahmed, Mahmoud.

In: Molecular Membrane Biology, Vol. 5, No. 1, 1983, p. 35-47.

Research output: Contribution to journalArticle

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