Solubilization of a stereospecific opiate-macromolecular complex from rat brain.
A [3H]etorphine-macromolecular complex has been solubilized from rat brain synaptosomal fraction by extraction with the nonionic detergent Brij 36T. Stereospecificity of binding to this solubilized complex was demonstrated by the finding that radioactivity in the complex was virtually eliminated when binding had occurred in the presence of excess levorphanol, an active narcotic analgesic, while it was unaffected by its inactive enantiomorph dextrorphan. Bound radioactivity was dissociated by proteolytic enzymes, sulfhydryl reagents, and heat, suggesting the presence of protein. The bound solubilized macromolecular moiety may be the opiate receptor.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism / Q000648:ultrastructure*; D001923:Brain Chemistry; D003902:Detergents; D003917:Dextrorphan / Q000378:metabolism; D005048:Etorphine / Q000378:metabolism*; D007981:Levorphanol / Q000378:metabolism; D009019:Morphinans / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*; D051381:Rats; D011955:Receptors, Drug; D012995:Solubility; D013237:Stereoisomerism; D013347:Subcellular Fractions / Q000378:metabolism; D013574:Synaptosomes / Q000378:metabolism
D003902:Detergents; D009019:Morphinans; D009419:Nerve Tissue Proteins; D011955:Receptors, Drug; D003917:Dextrorphan; D007981:Levorphanol; D005048:Etorphine