High-Affinity Binding of Ethacrynic Acid Is Mediated by the Two Most Important Drug Binding Sites of Human Serum Albumin

Pharmacology ◽  
1986 ◽  
Vol 32 (4) ◽  
pp. 208-213 ◽  
Author(s):  
Klaus J. Fehske ◽  
Walter E. Müller
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Ethacrynic Acid ◽  
Drug Binding ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
Drug Binding Sites ◽  
Important Drug

scholarly journals Relations between high-affinity binding sites for l-tryptophan, diazepam, salicylate and Phenol Red on human serum albumin

1983 ◽  
Vol 209 (1) ◽  
pp. 135-142 ◽  
Author(s):  
U Kragh-Hansen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Association Constants ◽  
The Other ◽  
Affinity Binding ◽  
Phenol Red ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site

Binding of L-tryptophan, diazepam, salicylate and Phenol Red to defatted human serum albumin was studied by ultrafiltration at pH 7.0. All ligands bind to one high-affinity binding site with association constants of the order of 10(4)-10(5)M-1. The number of secondary binding sites was found to vary from zero to five, with association constants about 10(3)M-1. Competitive binding studies with different pairs of the ligands were performed. Binding of both ligands was determined simultaneously. L-Tryptophan and diazepam were found to compete for a common high-affinity binding site on albumin. The following combinations of ligands do not bind competitively to albumin: L-tryptophan-Phenol Red, L-tryptophan-salicylate and Phenol Red-salicylate. On the other hand, high-affinity bindings of the three ligands do not take place independently but in such a way that binding of one of the ligands results in a decrease in binding of the other ligands. The decreases in binding are reciprocal and can be accounted for by introducing a coupling constant. The magnitude of the constant is dependent on the ligands being bound. In the present study, the mutual decrease in binding was more pronounced with L-tryptophan-salicylate and Phenol Red-salicylate than with L-tryptophan-Phenol Red.

scholarly journals Relations between high-affinity binding sites of markers for binding regions on human serum albumin

1985 ◽  
Vol 225 (3) ◽  
pp. 629-638 ◽  
Author(s):  
U Kragh-Hansen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Affinity Binding ◽  
Phenol Red ◽  
Coupling Constant ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site

Binding of warfarin, digitoxin, diazepam, salicylate and Phenol Red, individually or in different pair combinations, to defatted human serum albumin at ligand/protein molar ratios less than 1:1 was studied at pH 7.0. The binding was determined by ultrafiltration. Some of the experiments were repeated with the use of equilibrium dialysis in order to strengthen the results. Irrespective of the method used, all ligands bind to one high-affinity binding site with an association constant in the range 10(4)-10(6) M-1. High-affinity binding of the following pair of ligands took place independently: warfarin-Phenol Red, warfarin-diazepam, warfarin-digitoxin and digitoxin-diazepam. Simultaneous binding of warfarin and salicylate led to a mutual decrease in binding of one another, as did simultaneous binding of digitoxin and Phenol Red. Both effects could be accounted for by a coupling constant. The coupling constant is the factor by which the primary association constants are affected; in these examples of anti-co-operativity the factor has a value between 0 and 1. In the first example it was calculated to be 0.8 and in the latter 0.5. Finally, digitoxin and salicylate were found to compete for a common high-affinity binding site. The present findings support the proposal of four separate primary binding sites for warfarin, digitoxin (and salicylate), diazepam and Phenol Red. An attempt to correlate this partial binding model for serum albumin with other models in the literature is made.

scholarly journals Biological characteristics of two lysines on human serum albumin in the high-affinity binding of 4Z,15Z-bilirubin-IXα revealed by phage display

FEBS Journal ◽  
2011 ◽  
Vol 278 (21) ◽  
pp. 4100-4111 ◽  
Author(s):  
Ai Minomo ◽  
Yu Ishima ◽  
Ulrich Kragh-Hansen ◽  
Victor T. G. Chuang ◽  
Makiyo Uchida ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Phage Display ◽  
Human Serum ◽  
Biological Characteristics ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals Location of drug binding sites on human serum albumin.

1986 ◽  
Vol 34 (7) ◽  
pp. 2989-2993 ◽  
Author(s):  
KAZUO MARUYAMA ◽  
HIDEO NISHIGORI ◽  
MOTOHARU IWATSURU
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Drug Binding Sites

scholarly journals Long chain fatty acids alter the interactive binding of ligands to the two principal drug binding sites of human serum albumin

PLoS ONE ◽  
2017 ◽  
Vol 12 (6) ◽  
pp. e0180404 ◽  
Author(s):  
Keishi Yamasaki ◽  
Saya Hyodo ◽  
Kazuaki Taguchi ◽  
Koji Nishi ◽  
Noriyuki Yamaotsu ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Long Chain Fatty Acids ◽  
Drug Binding Sites ◽  
Long Chain ◽  
Chain Fatty Acids

Development of DNA Nanostructures for High-Affinity Binding to Human Serum Albumin

2017 ◽  
Vol 139 (21) ◽  
pp. 7355-7362 ◽  
Author(s):  
Aurélie Lacroix ◽  
Thomas G. W. Edwardson ◽  
Mark A. Hancock ◽  
Michael D. Dore ◽  
Hanadi F. Sleiman
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Affinity Binding ◽  
Dna Nanostructures ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals N-bromosuccinimide-oxidized human serum albumin as a tool for the determination of drug binding sites of human serum albumin.

1983 ◽  
Vol 31 (3) ◽  
pp. 971-978 ◽  
Author(s):  
HIROKO SAKAMOTO ◽  
IZUMI NAGATA ◽  
KIYOMI KIKUCHI ◽  
MASAKO AIDA ◽  
MASACHIKA IRIE
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Drug Binding Sites
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