Characterization of neuropeptide Y binding sites in rat cardiac ventricular membranes

Peptides ◽  
1990 ◽  
Vol 11 (3) ◽  
pp. 545-550 ◽  
Author(s):  
A. Balasubramaniam ◽  
S. Sheriff ◽  
D.F. Rigel ◽  
J.E. Fischer
Keyword(s):  
1993 ◽  
Vol 108 (2) ◽  
pp. 304-311 ◽  
Author(s):  
David A. Walsh ◽  
John Wharton ◽  
David R. Blake ◽  
Julia M. Polak

1992 ◽  
Vol 67 (05) ◽  
pp. 582-584 ◽  
Author(s):  
Ichiro Miki ◽  
Akio Ishii

SummaryWe characterized the thromboxane A2/prostaglandin H2 receptors in porcine coronary artery. The binding of [3H]SQ 29,548, a thromboxane A2 antagonist, to coronary arterial membranes was saturable and displaceable. Scatchard analysis of equilibrium binding showed a single class of high affinity binding sites with a dissociation constant of 18.5 ±1.0 nM and the maximum binding of 80.7 ± 5.2 fmol/mg protein. [3H]SQ 29,548 binding was concentration-dependently inhibited by thromboxane A2 antagonists such as SQ 29,548, BM13505 and BM13177 or the thromboxane A2 agonists such as U46619 and U44069. KW-3635, a novel dibenzoxepin derivative, concentration-dependently inhibited the [3H]SQ 29,548 binding to thromboxane A2/prosta-glandin H2 receptors in coronary artery with an inhibition constant of 6.0 ± 0.69 nM (mean ± S.E.M.).


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