Isolation and N-terminal amino acid sequence of an octopamine ligand binding protein

FEBS Lett. 1989 Dec 18;259(1):117-20. doi: 10.1016/0014-5793(89)81508-x.

Abstract

An octopamine receptor photoaffinity probe was used to label membranes from the light organs of Photinus pyralis, a tissue highly enriched in octopamine receptors. Labeling was concentrated in a glycoprotein of 75 +/- 2 kDa with lesser labeling of a 79 +/- 2 kDa component. Labeling could be displaced by prior incubation with octopamine, mianserin, cyproheptadine, phentolamine or propranolol, with a relative potency that correlated with the ability of these same agents to modulate light organ octopamine-sensitive adenylate cyclase. The 75 kDa binding protein was isolated and its N-terminal amino acid sequence was determined.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Affinity Labels
  • Amino Acid Sequence
  • Animals
  • Azides / metabolism
  • Coleoptera
  • Imidazoles / metabolism
  • Imidazolidines*
  • Molecular Sequence Data
  • Molecular Weight
  • Octopamine / metabolism*
  • Receptors, Adrenergic / isolation & purification*
  • Receptors, Adrenergic / metabolism
  • Receptors, Biogenic Amine*

Substances

  • Affinity Labels
  • Azides
  • Imidazoles
  • Imidazolidines
  • Receptors, Adrenergic
  • Receptors, Biogenic Amine
  • norsynephrine receptor
  • NC 5Z
  • Octopamine

Associated data

  • GENBANK/Y07523