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. 1981 Jul;78(7):4635–4638. doi: 10.1073/pnas.78.7.4635

Characterization and partial purification of solubilized active opiate receptors from toad brain.

U T Ruegg, S Cuenod, J M Hiller, T Gioannini, R D Howells, E J Simon
PMCID: PMC319848  PMID: 6270689

Abstract

Opiate receptors have been solubilized from toad brain membranes in active form by using digitonin. Between 40% and 50% of the stereospecific binding activity present in toad brain membranes is recoverable in the ultracentrifugal supernatant of digitonin extracts. Binding of opiates to the solubilized receptor is enhanced 4- to 5-fold by decreasing digitonin concentration to 0.1% or less prior to binding. The solubilized receptor is similar to the membrane-bound receptor in its affinity for various ligands and its sensitivity to heat, trypsin, and N-ethylmaleimide. Moreover, the sodium effect seen in membrane-bound receptor is retained in the solubilized preparation. Both membrane-bound and soluble toad receptors show weak binding of enkephalins, suggesting that they are predominantly of the mu type. The solubilized opiate receptor has an approximate molecular weight of 350,000-400,000. Purification of up to 20-fold has been achieved by gel filtration on Sepharose CL-6B.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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