Partial Purification of the Opioid Receptor from Human Placenta

  • Mahmoud S. Ahmed
  • Anna G. Cavinato
Part of the Trophoblast Research book series (TR)


The human placental villus tissue contains membrane bound etorphine binding sites (Valette et al., 1980). These sites were shown to have binding properties similar to those of the Kappa opioid receptor subtypes. We solubilized these receptors using the detergent 3-[(3-cholamidopropyl)-dimethylammonio]-1-propane sulfonate (CHAPS) (Ahmed et al., 1981). The binding activity was of a truly soluble proteindetergent macromolecular complex migrating on a Sepharose CL-6B column between two soluble proteins. The apparent Stokes radius of the complex was 70 Å (Ahmed, 1983). The solubilized receptors were shown to be all or in part a protein with an (SH) group at or close to the binding site. This group was found to be necessary for binding activity (Ahmed, 1983).


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Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • Mahmoud S. Ahmed
    • 1
  • Anna G. Cavinato
    • 1
  1. 1.Department of Biochemistry, College of MedicineUniversity of Tennesee Center for the Health SciencesMemphisUSA

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