1H NMR study of low-affinity binding of ibuprofen to human serum albumin at different pH

2000 ◽  
Vol 19 (2) ◽  
pp. 179-186 ◽  
Author(s):  
C. -G. Li ◽  
M. -L. Liu ◽  
C. -H. Ye
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
1H Nmr ◽  
Affinity Binding ◽  
Nmr Study

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

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

1H NMR Studies on the Interaction of β-Carboline Derivatives with Human Serum Albumin

1998 ◽  
Vol 130 (2) ◽  
pp. 281-286 ◽  
Author(s):  
Gianluigi Veglia ◽  
Maurizio Delfini ◽  
Maria Rosaria Del Giudice ◽  
Elena Gaggelli ◽  
Gianni Valensin
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
1H Nmr ◽  
Nmr Studies

scholarly journals Octanoate binding to the indole- and benzodiazepine-binding region of human serum albumin

1991 ◽  
Vol 273 (3) ◽  
pp. 641-644 ◽  
Author(s):  
U Kragh-Hansen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Equilibrium Dialysis ◽  
Affinity Binding ◽  
Experimental Conditions ◽  
High Affinity Binding ◽  
Molar Ratios ◽  
High Affinity ◽  
High Affinity Binding Site

Binding of L-tryptophan, diazepam and octanoate to defatted human serum albumin was studied at pH 7.0 by equilibrium dialysis at low ligand/protein molar ratios. L-Tryptophan binding takes place at only one site of the protein with an association constant of 4.4 x 10(4) M-1. Under the present experimental conditions, binding of diazepam and octanoate could be accounted for by high-affinity binding alone with primary association constants of 3.8 x 10(5) M-1 and 1.6 x 10(6) M-1 respectively. During the simultaneous presence of L-tryptophan plus octanoate or diazepam plus octanoate, pronounced mutual reductions in binding were observed. Analysis of the data suggests that the reductions in binding represent competition for a common high-affinity binding site. Thus a region seems to exist that is capable of binding one molecule of these diverse ligands with a high affinity. The location of this region within the albumin molecule is discussed.

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