Characterization of [125I]Endothelin-1 Binding Sites in Rat Cardiac Membrane Fragments

1989 ◽  
Vol 13 ◽  
pp. S171-173 ◽  
Author(s):  
Xin-Hua Gu ◽  
David J. Casley ◽  
Winifred G. Nayler
1984 ◽  
Vol 259 (24) ◽  
pp. 15013-15016 ◽  
Author(s):  
M L Garcia ◽  
M J Trumble ◽  
J P Reuben ◽  
G J Kaczorowski

1994 ◽  
Vol 26 (7) ◽  
pp. 915-923 ◽  
Author(s):  
Nancy Bowling ◽  
Gregory P. Dubé ◽  
William L. Kurtz ◽  
Kellie A. Brune ◽  
David L. Saussy ◽  
...  

1995 ◽  
Vol 26 ◽  
pp. S336-340
Author(s):  
Y. D. Zhao ◽  
D. R. Springall ◽  
Q. Hamid ◽  
M. H. Yacoub ◽  
M. Levene ◽  
...  

1995 ◽  
Vol 26 ◽  
pp. S336-340 ◽  
Author(s):  
Y. D. Zhao ◽  
D. R. Springall ◽  
Q. Hamid ◽  
M. H. Yacoub ◽  
M. Levene ◽  
...  

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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