Characterization of Local Polarity and Hydrophobic Binding Sites of β-Lactoglobulin by Using N-Terminal Specific Fluorescence Labeling

2006 ◽  
Vol 5 (1) ◽  
pp. 26-31 ◽  
Author(s):  
Su-Ying Dong ◽  
Zhen-Wen Zhao ◽  
Hui-Min Ma

2012 ◽  
Vol 26 (1) ◽  
pp. 36-40 ◽  
Author(s):  
O. Benjamin ◽  
M. Lassé ◽  
P. Silcock ◽  
D.W. Everett


1984 ◽  
Vol 231 (1) ◽  
pp. 144-157 ◽  
Author(s):  
Gregory A. Grabowski ◽  
Shimon Gatt ◽  
Joanne Kruse ◽  
Robert J. Desnick




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.).



1991 ◽  
Vol 53 (3) ◽  
pp. 325-331 ◽  
Author(s):  
Cynthia L. Woods ◽  
Christine Blazynski


1979 ◽  
Vol 254 (18) ◽  
pp. 8903-8908
Author(s):  
R.J. Cabelli ◽  
C.C. Malbon


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