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
2011 ◽  
Vol 284-286 ◽  
pp. 1764-1769 ◽  
Author(s):  
Vitalijs Lakevics ◽  
Janis Locs ◽  
Dagnija Loca ◽  
Valentina Stepanova ◽  
Liga Berzina-Cimdina ◽  
...  

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.


2010 ◽  
Vol 152-153 ◽  
pp. 1636-1640 ◽  
Author(s):  
Kong Yin Zhao ◽  
Jun Fu Wei ◽  
Jin Yang Zhou ◽  
Yi Ping Zhao ◽  
Guo Xiang Cheng

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.


2010 ◽  
Vol 93-94 ◽  
pp. 583-586 ◽  
Author(s):  
Tippavan Hongkachern ◽  
Verawat Champreda ◽  
Toemsak Srikhirin ◽  
Thidarat Wangkam ◽  
Tanakorn Osotchan

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.


Soft Matter ◽  
2021 ◽  
Author(s):  
Priyanshi Agnihotri ◽  
Sangeeta Jangra ◽  
Shikha Aery ◽  
Abhijit Dan

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)...


1983 ◽  
Vol 61 (2) ◽  
pp. 356-361 ◽  
Author(s):  
S. F. Sun ◽  
T. S. Chang ◽  
G. M. Lam

Difference spectra of tyrosyl residues in bovine serum albumin produced by three organic solvents (ethanol, n-propanol, and dioxane) have been studied at three different pH values (pH 2.2, pH 5.4–5.8, and pH 11.6). The measurements were taken at 25 °C and ionic strength 0.03 and in a concentration of organic solvent from 5% to 25% by volume. The spectra are compared to those of a model chromophore, N-acetyl-L-tyrosine ethyl ester. Both n-propanol and dioxane cause a change in the conformation of the protein, while ethanol does not. Near the isoelectric point the difference spectra produced by n-propanol (at high concentration) and dioxane appear to be the results of a superposition of denaturation blue shifts on solvent-induced red-shifts; those produced by ethanol are characteristic of perturbation of tyrosyl and tryptophyl residues. An empirical equation which correlates Δε (the molar difference absorption coefficient) with n (refractive index) and D (dielectric constant) is proposed to interpret the results qualitatively.


2010 ◽  
Vol 297 (1) ◽  
pp. 126-137 ◽  
Author(s):  
Kongyin Zhao ◽  
Guoxiang Cheng ◽  
Junfu Wei ◽  
Jinyang Zhou ◽  
Jinlong Zhang ◽  
...  

2012 ◽  
Vol 625 ◽  
pp. 206-209
Author(s):  
Wen Kui Cui ◽  
Kong Yin Zhao ◽  
Jun Fu Wei ◽  
Guo Xiang Cheng

Calcium polyacrylate/alginate (CPA/A) hybrid polymer microspheres with the imprinting of bovine serum albumin (BSA) were prepared via Ca2+ crosslinking of sodium polyacrylate (SPA), BSA and sodium alginate (SA) in inverse suspension. The specific rebinding properties of BSA imprinted hydrogel microspheres (CPA/A MIPMs) were investigated by controlling pH value from the viewpoint of adjusting the process of gelling, removing template and rebinding. The optimized pH values in gelling, removing template and rebinding process was 4.1, 8.3 and 4.2, respectively.


2011 ◽  
Vol 694 ◽  
pp. 160-164 ◽  
Author(s):  
Yong Liu ◽  
Yan Sun ◽  
Yan Li Li ◽  
Shao Chun Xu ◽  
Yao Xing Xu

In this paper, the properties of chitosan nanoparticles and bovine serum albumin-loaded chitosan nanoparticles prepared with sodium tripolyphosphate at different pH values were discussed. Interactions in chitosan nanoparticles and bovine serum albumin-loaded chitosan nanoparticles were analyzed by Fourier transform infrared spectroscopy and differential scanning calorimetry. The results indicated that there were more complicated interactions in chitosan nanoparticles prepared at different pH values. When the pH values were lower or higher than isoelectric point value of target protein (bovine serum albumin), the big different interactions occurred in chitosan nanoparticles. These differences also would result in different releasing properties.


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