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
Keyword(s):  
Binding Sites ◽  
Fluorescence Labeling ◽  
Specific Fluorescence ◽  
Hydrophobic Binding ◽  
Β Lactoglobulin

Human lysosomal β-glucosidase: Kinetic characterization of the catalytic, aglycon, and hydrophobic binding sites

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

Characterization of Thromboxane A2/Prostaglandin H2 Receptors in Porcine Coronary Artery -The Inhibitory Effect of a Novel Dibenzoxepin Derivative, KW-3635

1992 ◽  
Vol 67 (05) ◽  
pp. 582-584 ◽  
Author(s):  
Ichiro Miki ◽  
Akio Ishii
Keyword(s):  
Coronary Artery ◽  
Binding Sites ◽  
Thromboxane A2 ◽  
Inhibitory Effect ◽  
Scatchard Analysis ◽  
Single Class ◽  
Porcine Coronary Artery ◽  
Equilibrium Binding ◽  
H2 Receptors

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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