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Complex Interaction of α2-Adrenoceptor Binding Sites with Bovine Brain and Lung Extracts Containing Clonidine-Displacing Substance

  • D. Pinthong
  • , D. A. Kendall
  • , V. G. Wilson
  • Nottingham University Hospitals NHS Trust

Research output: Contribution to journal › Article › peer-review

Abstract

Previous studies have established that methanolic extracts of bovine brain and lung possess CDS activity with an agonist-like profile at α 2-adrenoceptor binding sites (i.e., greater potency against [ 3H]-clonidine sites than against [3H]-RX-821001 sites). Following prolonged reflux in ethylacetate, monovalent cations and histamine were removed from the lung extract, and the resulting extract exhibited similar potency against both radioligands, indicative of an antagonist-like profile. These observations help explain the absence of biologic activity at α 2-adrenoceptors in the methanolic extracts as reported in our companion paper.

Original languageEnglish
Pages (from-to)216-221
Number of pages6
JournalAnnals of the New York Academy of Sciences
Volume1009
DOIs
Publication statusPublished - 2003
Externally publishedYes

Keywords

  • Clonidine-displacing substance
  • α-adrenoceptor binding sites

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