scholarly journals Studies on the mechanism of binding of serum albumins to immobilized cibacron blue F3G A

1980 ◽  
Vol 189 (1) ◽  
pp. 27-34 ◽  
Author(s):  
R J Leatherbarrow ◽  
P D Dean
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Serum Albumins ◽  
Fatty Acid Binding ◽  
Cibacron Blue ◽  
Structural Analogues ◽  
Bilirubin Binding ◽  
Sepharose 4B

The interaction of Cibacron Blue F3G A-Sepharose 4B with several serum albumins was studied. Although all albumins used were fond to bind to this adsorbent, human serum albumin was bound to a far greater extent than were the others. From the results of competition experiments and n.m.r. studies of Cibacron Blue and/or bilirubin binding to human serum albumin it is proposed that the mechanism of the interaction between human serum albumin and cibacron Blue is consistent wit Cibacron Blue binding to bilirubin-binding sites. In contrast with these findings with human serum albumin, there is little or no interaction of Cibacron Blue and the bilirubin-binding sites of albumins from rabbit, horse, bovine or sheep sera, although some interaction occurs between Cibacron Blue and the fatty acid-binding sites of these proteins. Structural analogues of Cibacron Blue have been used to investigate the binding of albumins to these ligands.

scholarly journals The effect of ligand presaturation on the interaction of serum albumins with an immobilized Cibacron Blue 3G-A studied by affinity gel electrophoresis

1981 ◽  
Vol 199 (3) ◽  
pp. 465-472 ◽  
Author(s):  
E C Metcalf ◽  
B Crow ◽  
P D G Dean
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Dissociation Constant ◽  
Gel Electrophoresis ◽  
Dissociation Constants ◽  
Serum Albumins ◽  
Albumin Ratio ◽  
Cibacron Blue ◽  
Affinity Gel Electrophoresis

The interaction of the immobilized triazine dye Cibacron Blue 3G-A with rat, rabbit, sheep, goat, bovine and human serum albumins was studied by affinity gel electrophoresis. Dissociation constants were estimated in each instance and showed human serum albumin to have a significantly higher affinity for the dye than did albumin from any other species. Pretreatment of the defatted proteins with bilirubin (3 mol of bilirubin/mol of protein) did not increase the dissociation constants of the serum albumins, whereas pretreatment with palmitate (7 mol of palmitate/mol of protein) increased the dissociation constant in all cases: 3-fold for human serum albumin, 15-fold for other serum albumins. Increasing the bilirubin/albumin ratio (to 7:1) did not affect the dissociation constant of the albumins studied. Decreasing the palmitate/albumin ratio decreased the dissociation constant for human serum albumin, but did not affect those of bovine and rat albumins. Altering the chain length of the presaturating fatty acid dramatically changed the dissociation constant of both human and bovine serum albumins. Butyrate, hexanoate, octanoate and decanoate did not significantly influence the dissociation constants of bovine and human serum albumins for Cibacron Blue, whereas laurate, myristate and palmitate greatly increased the dissociation constant. These data are discussed in relationship to the behaviour of albumins during dye--agarose column chromatography. In Addendum the effect of nucleotide presaturation on the interaction between Bacillus stearothermophilus 6-phosphogluconate dehydrogenase and the immobilized triazine dyes Cibacron Blue 3G-A and Procion Red HE-3B was examined, and the implications for dye--ligand chromatography are discussed.

scholarly journals Evidence that Chemical Chaperone 4-Phenylbutyric Acid Binds to Human Serum Albumin at Fatty Acid Binding Sites

PLoS ONE ◽  
2015 ◽  
Vol 10 (7) ◽  
pp. e0133012 ◽  
Author(s):  
Debasish Roy ◽  
Vinod Kumar ◽  
Joel James ◽  
Mohamed Sham Shihabudeen ◽  
Shweta Kulshrestha ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Chemical Chaperone ◽  
Fatty Acid Binding ◽  
Phenylbutyric Acid

scholarly journals Localizing Fatty Acid Binding Sites on Human Serum Albumin by 2D-NMR

2009 ◽  
Vol 96 (3) ◽  
pp. 442a
Author(s):  
Eileen Krenzel ◽  
Zhongjing Chen ◽  
James A. Hamilton
Keyword(s):  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
2D Nmr ◽  
Fatty Acid Binding

scholarly journals Influence of mutations caused by radiation exposure on the bilirubin binding sites of human serum albumin

2021 ◽  
Vol 18 (1) ◽  
pp. 46-57
Author(s):  
V. V. Poboinev ◽  
V. V. Khrustalev ◽  
A. N. Stojarov ◽  
T. A. Khrustaleva
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Radiation Exposure ◽  
Human Serum ◽  
Binding Sites ◽  
Amino Acid Substitutions ◽  
Amino Acid Residues ◽  
Bilirubin Binding

In this article we analyze the bilirubin binding sites of human serum albumin from the point of view of the secondary structure instability, as well as the effect of amino acid substitutions caused by radiation exposure on the ability of albumin to bind bilirubin-IX-alpha. Based on calculations of binding energy and inhibition constants of bilirubin-albumin complexes before and after the amino acid substitutions, it was found that amino acid substitutions have different effects on the ability of human serum albumin to bind bilirubin. Amino acid substitutions Asp269-Gly269 (Nagasaki-1), Glu354-Lys354 (Hiroshima-1), Asp375-Asn375 (Nagasaki-2) reduce the binding free energy of bilirubin with human serum albumin, and the amino acid substitutions His3-Gln3 (Nagasaki-3) and Glu382-Lys382 (Hiroshima-2) increase it during molecular docking with the corresponding areas of the protein surface. The inhibition constants are significantly higher than with known binding sites. In general, mutations caused by radiation exposure cannot effect on bilirubin binding sites of human serum albumin, since the amino acid residues that are replaced do not interact with the amino acid residues from the binding sites (Leu115, Arg117, Phe134, Tyr138, Ile142, Phe149, Phe157, Tyr161, Arg186, Lys190, Lys240, Arg222). All amino acid residues from known binding sites are located in stable elements of the secondary structure of human serum albumin.The data obtained are important for understanding the impact of radiation exposure on the development of bilirubin encephalopathy in the population of the Chernobyl region and Japan.

scholarly journals Relative Affinities of Fatty Acid Binding Sites on Human Serum Albumin Probed by 2D-NMR

2011 ◽  
Vol 100 (3) ◽  
pp. 551a
Author(s):  
Eileen Krenzel ◽  
Zhongjing Chen ◽  
James A. Hamilton
Keyword(s):  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
2D Nmr ◽  
Fatty Acid Binding

scholarly journals Dansylation of human serum albumin in the study of the primary binding sites of bilirubin and l-tryptophan

1979 ◽  
Vol 181 (1) ◽  
pp. 251-253 ◽  
Author(s):  
C Jacobsen ◽  
J Jacobsen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Sites ◽  
Lysine Residue ◽  
Bilirubin Binding ◽  
Albumin Molecule ◽  
Common Cavity

Binding of bilirubin and of L-tryptophan to dansylated albumins was investigated. Dansylation of less than one lysine residue per molecule of albumin did not affect the bilirubin binding, but decreased the L-tryptophan binding, indicating that dansylation had taken place in or near the l-tryptophan-binding site. Native albumin and albumin-bilirubin 1:1 complex showed the same affinity for L-tryptophan. The results indicate that, although L-tryptophan and bilirubin are bound in the same region, perhaps in a common cavity of the albumin molecule, such a cavity is sufficiently large to contain both ligands.

scholarly journals Comparative studies of the binding of some ligands to human serum albumin non-covalently attached to immobilized Cibacron Blue, or covalently immobilized on Sepharose, by column affinity chromatography

1983 ◽  
Vol 213 (2) ◽  
pp. 387-390 ◽  
Author(s):  
C Lagercrantz ◽  
T Larsson
Keyword(s):  
Fatty Acids ◽  
Salicylic Acid ◽  
Human Serum Albumin ◽  
Complex Formation ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Strength ◽  
Cibacron Blue

A comparative study of the ligand-binding properties of human serum albumin was performed by the technique of affinity chromatography with the protein attached to immobilized Cibacron Blue F3GA (Blue Sepharose), or covalently immobilized on Sepharose. The binding strength of octanoate, decanoate and dodecanoate is much weaker when human serum albumin is attached to immobilized Cibacron Blue, indicating that the binding sites for fatty acids are involved in the attachment of human serum albumin to immobilized Cibacron Blue. The results revealed additional alterations of the ligand binding when human serum albumin was attached to immobilized Cibacron Blue, involving sites outside of the binding domains of fatty acids. Thus the stereoselective binding of L-tryptophan was abolished, and the resolution of the warfarin enantiomers was impaired. However, the binding strength of warfarin and salicylic acid was rather close to the values observed with human serum albumin covalently immobilized on Sepharose. It is suggested that the availability of the binding sites for L-tryptophan, warfarin and salicylic acid is partially blocked by the complex between albumin and the dye without direct participation in the complex-formation. An alternative interpretation involves an allosteric mechanism brought about by complex-formation between serum albumin and the immobilized Cibacron Blue.

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