Influence of mixed electrolytes and pH on adsorption of bovine serum albumin in hydrophobic interaction chromatography

2017 ◽  
Vol 1521 ◽  
pp. 73-79 ◽  
Author(s):  
Eva Hackemann ◽  
Hans Hasse
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Hydrophobic Interaction ◽  
Bovine Serum ◽  
Hydrophobic Interaction Chromatography ◽  
Mixed Electrolytes

scholarly journals Insight into the Molecular Interaction of Cloxyquin (5-chloro-8-hydroxyquinoline) with Bovine Serum Albumin: Biophysical Analysis and Computational Simulation

2019 ◽  
Vol 21 (1) ◽  
pp. 249 ◽  
Author(s):  
Kamonrat Phopin ◽  
Waralee Ruankham ◽  
Supaluk Prachayasittikul ◽  
Virapong Prachayasittikul ◽  
Tanawut Tantimongcolwat
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Hydrophobic Interaction ◽  
Bovine Serum ◽  
Computational Simulation ◽  
Docking Simulation ◽  
Biophysical Model ◽  
Therapeutic Drug ◽  
Fatty Acid Binding ◽  
Binding Behavior

Cloxyquin is a potential therapeutic compound possessing various bioactivities, especially antibacterial, antifungal, cardioprotective, and pain relief activities. Herein, the interaction mechanism between cloxyquin and bovine serum albumin (BSA) has been elucidated in order to fulfill its pharmacokinetic and pharmacodynamic gaps essential for further development as a therapeutic drug. Multi-spectroscopic and biophysical model analysis suggested that cloxyquin interacts with BSA via a static process by ground-state complex formation. Its binding behavior emerged as a biphasic fashion with a moderate binding constant at the level of 104 M−1. Thermodynamic analysis and molecular docking simulation concurrently revealed that hydrophobic interaction is a major driving force for BSA–cloxyquin complexation. Binding of cloxyquin tends to slightly enlarge the monomeric size of BSA without a significant increase of aggregate fraction. Cloxyquin preferentially binds into the fatty acid binding site 5 (FA5) of the BSA via hydrophobic interaction amongst its quinoline scaffold and Phe550, Leu531, and Leu574 residues of BSA. The quinoline ring and hydroxyl moiety of cloxyquin also form the π–π interaction and the hydrogen bond with Phe506. Our data indicate a potential function of serum albumin as a carrier of cloxyquin in blood circulation.

Study of hydrophobic interaction adsorption of bovine serum albumin under overloaded conditions using flow microcalorimetry

1999 ◽  
Vol 865 (1-2) ◽  
pp. 111-122 ◽  
Author(s):  
Maria A Esquibel-King ◽  
Ana Cristina Dias-Cabral ◽  
Joao A Queiroz ◽  
Neville G Pinto
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Hydrophobic Interaction ◽  
Bovine Serum ◽  
Flow Microcalorimetry

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

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