scholarly journals Characterization of gonadotropin binding sites in the intracellular organelles of bovine corpora lutea and comparison with plasma membrane sites.

1981 ◽  
Vol 256 (6) ◽  
pp. 2628-2634
Author(s):  
C.V. Rao ◽  
S. Mitra ◽  
F.R. Carman
1987 ◽  
Vol 19 (10) ◽  
pp. 957-962 ◽  
Author(s):  
Miguel Trueba ◽  
JoséMaría Guantes ◽  
Ana Isabel Vallejo ◽  
María JoséSancho ◽  
Aida Marino ◽  
...  

1989 ◽  
Vol 8 (4) ◽  
pp. 229-239 ◽  
Author(s):  
Miguel Trueba ◽  
IÑAki Ibarrola ◽  
Ana Isabel Vallejo ◽  
MarÍA José Sancho ◽  
Aida Marino ◽  
...  

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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