Odorant-binding protein. Characterization of ligand binding

J. Pevsner, V. Hou, A. M. Snowman, S. H. Snyder

Research output: Contribution to journalArticle

124 Scopus citations

Abstract

We have characterized the odorant binding properties of purified bovine odorant-binding protein (OBP) using as a ligand [3H]3,7-dimethyloctan-1-ol ([3H]DMO). A broad variety of odorants, including terpenes, aldehydes, esters, and musks, bind to OBP with affinities of 0.2 to 100 μM. Odorant affinities for OBP correlate most closely with their stimulation of an odorant-sensitive adenylyl cyclase as well as hydrophobicity. We also measured the kinetics of binding for the ligands, [3H]DMO and 2-isobutyl-3-[3H]methoxypyrazine. Dissociation of both is markedly accelerated in the presence of excess unlabeled ligand. Competition curves of displacers for [3H]DMO binding are shallow, and saturation binding isotherms for 3H-odorants are curvilinear. These kinetic and equilibrium binding properties suggest that OBP interactions with odorant ligands are negatively cooperative.

Original languageEnglish (US)
Pages (from-to)6118-6125
Number of pages8
JournalJournal of Biological Chemistry
Volume265
Issue number11
StatePublished - May 16 1990

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Pevsner, J., Hou, V., Snowman, A. M., & Snyder, S. H. (1990). Odorant-binding protein. Characterization of ligand binding. Journal of Biological Chemistry, 265(11), 6118-6125.