Solubilization of rat liver alpha 1-adrenergic receptors. Agonist specific alteration in receptor binding affinity.

Published

Journal Article

An improved method for the solubilization of the alpha 1-adrenergic receptors in rat liver, utilizing digitonin, glycerol and sonication, is described. The yield of solubilized receptors was approximately 20%. The soluble receptors showed characteristics similar to the membrane-bound alpha 1 receptors. However, upon solubilization, the affinity for the agonists (-)norepinephrine and (-)epinephrine increased 35- to 66-fold when compared to the affinity in the membranes. The affinity for antagonists remained unchanged. A number of synthetic partial agonists showed a less marked (5- to 10-fold) increase in affinity upon solubilization. These data are consistent with the notion that these receptors might be capable of existing in two distinct conformational states with the high affinity state for agonists being favored by solubilization.

Full Text

Duke Authors

Cited Authors

  • Wikberg, JE; Lefkowitz, RJ; Caron, MG

Published Date

  • November 1, 1983

Published In

Volume / Issue

  • 32 / 21

Start / End Page

  • 3171 - 3178

PubMed ID

  • 6139112

Pubmed Central ID

  • 6139112

International Standard Serial Number (ISSN)

  • 0006-2952

Digital Object Identifier (DOI)

  • 10.1016/0006-2952(83)90200-9

Language

  • eng

Conference Location

  • England