Spectroscopic Characterization of the Heme-Binding Sites inPlasmodium falciparumHistidine-Rich Protein 2†

Biochemistry ◽  
1999 ◽  
Vol 38 (51) ◽  
pp. 16916-16924 ◽  
Author(s):  
Clara Y. H. Choi ◽  
Jose F. Cerda ◽  
Hsiu-An Chu ◽  
Gerald T. Babcock ◽  
Michael A. Marletta
Biochemistry ◽  
1974 ◽  
Vol 13 (6) ◽  
pp. 1075-1082 ◽  
Author(s):  
Lynne M. Angerer ◽  
S. Georghiou ◽  
E. N. Moudrianakis

Biochemistry ◽  
2011 ◽  
Vol 50 (42) ◽  
pp. 9036-9045 ◽  
Author(s):  
Juliette Trepreau ◽  
Eve de Rosny ◽  
Carole Duboc ◽  
Géraldine Sarret ◽  
Isabelle Petit-Hartlein ◽  
...  

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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