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 language | English (US) |
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Pages (from-to) | 701-703 |
Number of pages | 3 |
Journal | Peptides |
Volume | 10 |
Issue number | 3 |
DOIs | |
State | Published - 1989 |
Keywords
- B bradykinin receptor
- Nasal turbinate
- [H]Bradykinin binding
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Endocrinology
- Cellular and Molecular Neuroscience