Biochemical characterization of histamine H1 receptors in bovine adrenal medulla

Biochem Biophys Res Commun. 1991 Jun 28;177(3):1233-9. doi: 10.1016/0006-291x(91)90673-u.

Abstract

Bovine adrenal medullary membranes display high affinity and saturable binding to [3H]mepyramine, a selective H1 antagonist, with Kd of 1.5 +/- 0.1 nM and Bmax of 694 +/- 12 fmol/mg protein. [3H]Azidobenzpyramine, an azidobenzamide derivative of mepyramine, was synthesized and used to photolabel the high affinity mepyramine binding sites. Following photolysis, a protein component with an approximate molecular weight of 53-58 kDa was shown to be covalently labeled, as judged by gel filtration and SDS/PAGE; labeling being greatly reduced in the presence of excess unlabeled mepyramine. These results indicate that bovine adrenal medulla expresses a large number of H1 receptors, which are pharmacologically and biochemically indistinguishable from the H1 receptor of many other tissues of various species.

MeSH terms

  • Adrenal Medulla / metabolism*
  • Affinity Labels / metabolism
  • Animals
  • Azides / metabolism*
  • Binding, Competitive
  • Cattle
  • Cell Membrane / metabolism
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Kinetics
  • Molecular Weight
  • Photolysis
  • Pyrilamine / analogs & derivatives*
  • Pyrilamine / metabolism*
  • Receptors, Histamine H1 / isolation & purification
  • Receptors, Histamine H1 / metabolism*

Substances

  • Affinity Labels
  • Azides
  • Receptors, Histamine H1
  • 4-azidobenzpyramine
  • Pyrilamine