scholarly journals Examination of the Effects of Activated Carbon Produced from Coal Using Single-Step H3PO4/N2+H2O Vapor Activation on the Adsorption of Bovine Serum Albumin at Different Temperatures and pH Values

2017 ◽  
pp. 219-236 ◽  
Author(s):  
Atakan Toprak
Keyword(s):  
Activated Carbon ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Single Step ◽  
Ph Values ◽  
Different Temperatures

Temperature- and pH-responsive poly(N-isopropylacrylamide-co-methacrylic acid) microgels as a carrier for controlled protein adsorption and release

Soft Matter ◽  
2021 ◽  
Author(s):  
Priyanshi Agnihotri ◽  
Sangeeta Jangra ◽  
Shikha Aery ◽  
Abhijit Dan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Adsorption ◽  
Methacrylic Acid ◽  
Bovine Serum ◽  
Ph Responsive ◽  
Ph Values ◽  
Different Temperatures ◽  
Adsorption And Release

Herein, we report controlled protein adsorption and delivery of thermo- and pH-responsive poly(N-isopropylacrylamide-co-methacrylic acid) (PNIPAM-co-MAA) microgels at different temperatures, pH values and ionic strengths by employing bovine serum albumin (BSA)...

Effect of the Association of Eosin Molecules on Their Interaction with Bovine Serum Albumin at Various pH Values

2019 ◽  
Vol 86 (5) ◽  
pp. 855-860
Author(s):  
E. S. Gorodnichev ◽  
A. A. Kuleshova ◽  
A. V. Bykov ◽  
A. M. Saletsky
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ph Values

Bioceramic Hydroxyapatite Granules for Purification of Biotechnological Products

2011 ◽  
Vol 284-286 ◽  
pp. 1764-1769 ◽  
Author(s):  
Vitalijs Lakevics ◽  
Janis Locs ◽  
Dagnija Loca ◽  
Valentina Stepanova ◽  
Liga Berzina-Cimdina ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Phosphate Buffer Solution ◽  
Sorption Process ◽  
Buffer Solution ◽  
Ph Values ◽  
Bovine Serum Albumin Adsorption ◽  
Albumin Adsorption

Sorption experiments of bovine serum albumin (BSA) on hydroxyapatite (HAp) ceramic granules, prepared at three temperatures 900°C, 1000°C and 1150°C were performed at room temperature 18,6 °C and phosphate buffer, pH 5,83; 6.38 and 7,39. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HAp ceramics specific surface area and pH values of phosphate buffer solution. However, it was confirmed that granule size was also an important parameter for bovine serum albumin adsorption. As a result of these experiments, the most appropriate adsorption conditions and phosphate buffer pH values influence on to BSA sorption were analyzed.

The Rebinding Properties of Bovine Serum Albumin Imprinted Calcium Phosphate/Polyacrylate/Alginate Hybrid Polymer Microspheres

2010 ◽  
Vol 152-153 ◽  
pp. 1636-1640 ◽  
Author(s):  
Kong Yin Zhao ◽  
Jun Fu Wei ◽  
Jin Yang Zhou ◽  
Yi Ping Zhao ◽  
Guo Xiang Cheng
Keyword(s):  
Calcium Phosphate ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Polymer Microspheres ◽  
Hybrid Polymer ◽  
Ph Values ◽  
Factors Influencing ◽  
Recognition Property ◽  
Template Protein

Calcium phosphate/polyacrylate/alginate hybrid polymer microspheres with bovine serum albumin (BSA) embedded and coated on the surface were prepared with (NH4)2HPO4, sodium polyacrylate (SPA) and sodium alginate (SA) via Ca2+ crosslinking in inverse suspension. Rebinding behaviors of the microspheres were evaluated. The factors influencing the imprinting efficiency (IE) of imprinted microspheres were also studied, including the concentration of CaCl2, template content and pH values in rebinding solutions. Selectivity tests showed that the imprinted microspheres exhibited good recognition property for the template protein.

scholarly journals Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-5
Author(s):  
K. Grigoryan ◽  
H. Shilajyan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Ion Binding ◽  
Fluorescence Energy Transfer ◽  
Iodide Ion ◽  
Different Temperatures ◽  
Fluorescence Energy

The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change (), enthalpy change (), and entropy change (), at different temperatures (293, 298, and 303 K) were calculated, which indicated that the hydrophobic and electrostatic interactions were the predominant operating forces. The binding locality distance r between BSA and tri-iodide ion at different temperatures was determined based on Förster nonradiation fluorescence energy transfer theory.

Effect of pH on the Formation of a Bovine Serum Albumin Layer on a Poly(stryren-co-maleic Acid) Surface

2010 ◽  
Vol 93-94 ◽  
pp. 583-586 ◽  
Author(s):  
Tippavan Hongkachern ◽  
Verawat Champreda ◽  
Toemsak Srikhirin ◽  
Thidarat Wangkam ◽  
Tanakorn Osotchan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Maleic Acid ◽  
Bovine Serum ◽  
Quartz Crystal ◽  
Ph Value ◽  
Layer Formation ◽  
Force Microscopy ◽  
Ph Values ◽  
Atomic Force

The layer formation of bovine serum albumin (BSA) on a poly(styrene-co-maleic acid) (PSMA) surface was investigated by using quartz crystal microbalance (QCM) technique at various pH values. The formation of a BSA surface was examined by atomic force microscopy (AFM). To study the effect on the layer formation, the pH of solution was varied from 2 to 7.4 while the concentration of BSA was in the range of 0.01 to 5 mg/ml during the layer absorption. It was found that the BSA adsorption strongly depends on the pH of solution, and the concentration of BSA. The absorption layer occurred maximum at the pH value of 3.5 which resulted from the charge of PSMA and BSA molecules. The layer formation reached the saturate value at the concentration higher than 3 mg/ml. The molecular packing of the BSA layer at different pH values was determined by AFM and total mass change of QCM.

scholarly journals Spectroscopic Studies of the Interaction between Metformin Hydrochloride and Bovine Serum Albumin

2012 ◽  
Vol 11 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Ahmad Tanwir ◽  
Rahat Jahan ◽  
Mohiuddin Abdul Quadir ◽  
Mohammad A Kaisar ◽  
Md Khalid Hossain
Keyword(s):  
Hydrogen Bond ◽  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies ◽  
Metformin Hydrochloride ◽  
Tryptophan Residue ◽  
Different Temperatures ◽  
Hoff Equation

The affinity of a drug to serum albumin has influence on the pharmacokinetics of a drug. In the present study, the mutual interaction of metformin hydrochloride (MET) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under different conditions. It was observed that the fluorescence  quenching of BSA by metformin hydrochloride is a result of the formation of metformin hydrochloride- BSA complex with probable involvement of tryptophan residue. Fluorescence quenching constants were determined using  the Stern- Volmer equation and Van’t Hoff equation to provide a measure of the thermodynamic parameters ?G, ?H, and ?S at different temperatures indicating that the hydrogen bond and the hydrophobic forces play a major role for metformin hydrochloride- BSA association. DOI: http://dx.doi.org/10.3329/dujps.v11i1.12486 Dhaka Univ. J. Pharm. Sci. 11(1): 45-49, 2012 (June)

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