Identification of B2 bradykinin binding sites in the guinea pig nasal turbinate

Yutaka Fujiwara, John W Bloom, Charles R. Mantione, Henry I. Yamamura

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Specific high affinity BK binding sites in the nasal turbinate of the guinea pig have been demonstrated. Specific [3H]BK binding (10-330 pM) was saturable, and nonlinear least squares analysis indicated the presence of a high affinity binding site with a Kd value of 60 (50-78) pM and a Bmax value of 13.1±2.0 fmol/mg protein. In inhibition experiments, D-Phe7-BK (a B2 antagonist) inhibited [3H]BK binding with a Ki value of 23 nM, while des-Arg9[Leu8]-BK (a B1 antagonist) had no effect up to a concentration of 10 μM. These studies indicate the presence of B2 BK receptors in the guinea pig nasal turbinate.

Original languageEnglish (US)
Pages (from-to)701-703
Number of pages3
JournalPeptides
Volume10
Issue number3
DOIs
Publication statusPublished - 1989

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Keywords

  • B bradykinin receptor
  • Nasal turbinate
  • [H]Bradykinin binding

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

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