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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Jan;83(1):67–71. doi: 10.1073/pnas.83.1.67

Characterization of solubilized human and rat brain beta-endorphin-receptor complex.

D M Helmeste, C H Li
PMCID: PMC322792  PMID: 3001726

Abstract

Opioid receptors have been solubilized from human striatal and rat whole-brain membranes by use of 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Tritiated human beta-endorphin (3H-beta h-EP) binding revealed high-affinity competition by morphine, naloxone, and various beta-EP analogues, suggesting predominantly mu-type binding. Lack of high-affinity competition by (+/-)-3,4-dichloro-N-methyl-N-[2-(1-pyrrolidinyl)cyclohexyl]benzeneaceta mide methanesulfonate (U50-488, Upjohn) indicated that kappa sites were not labeled by 3H-beta h-EP under these conditions. Affinities were similar in both soluble and membrane preparations except for [Met]enkephalin, which appears to be rapidly degraded by the solubilized extract. Size differences between human and rat solubilized 3H-beta h-EP-receptor complexes were revealed by exclusion chromatography.

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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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