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Search Results: 1 - 10 of 3877 matches for " bovine serum albumin "
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(E)-2-Benzylidenecycloalkanones XII.* Kinetic Measurement of Bovine and Human Serum Albumine Interaction with Selected Chalcones and Their Cyclic Chalcone Analogues by UV Spectrophotometry  [PDF]
Beáta Veliká, Vladimíra Tome?ková, Krisztina Fodor, Ivan Kron, Pál Perjési
Spectral Analysis Review (SAR) , 2015, DOI: 10.4236/sar.2015.31001
Abstract: UV-VIS spectroscopic investigations of interaction of bovine and human serum albumin with selected chalcones (1) and their cyclic chalcone analogues: (E)-2-(4’-X-benzylidene-1-tetralones (3), benzosuberones (4) with dimethylamino and methoxy substituents and (E)-2-(2’,4’-dimethox- ybenzylidene)-1-indanone (2) were performed in polar respiration medium. Absorption maxima of the tested compounds were investigated in the presence of bovine and human serum albumin at the 0, 10, 30 and 60 minute timepoints of the interaction. The absorbance of all studied compounds in the presence of proteins decreased after one hour of the reaction. Molecule 4a showed the strongest and fastest kinet initial interaction with both albumins.
Using of In-Situ Mercury Film Sensor Hyphenated with Affinity Voltammetry for High Throughput Drug-Protein Binding Studies  [PDF]
Ahmed K. Youssef, Deia Abd El-Hady
American Journal of Analytical Chemistry (AJAC) , 2013, DOI: 10.4236/ajac.2013.44021
Abstract:

A new simple and reliable in-situ mercury film sensor coupled with affinity differential pulse stripping voltammetry (ADSPV) or affinity cyclic voltammetry (ACV) was investigated. The interaction of fenoprofen with bovine serum albumin (BSA) onto the proposed electrochemical sensor was studied. The nature of the electrochemical process of fenoprofen by cyclic voltammetry was depicted. Reproducibility of the proposed method was checked giving a precision of 0.073 standard deviation. The limit of detection and limit of quantification were 7.0 and 22.0 nmol/L, respectively. Fenoprofen was interacted with BSA by 1:1 stoichiometry to form electroinactive supramolecular complex. The binding constant was precisely estimated by non-linear regression analysis based on the shifting of analyte peak potentials. The proposed experiments and data analysis could be used to investigate the drug-protein binding constant within a short analysis time compared to other chromatographic techniques.

Preparation and Release Properties of Sol-Gel Encapsulated Proteins  [PDF]
Yu-Cheng Chen, Ching-Piao Liu, Chun-Kai Yang, Bao-Yu Huang, Chuen-Ying Liu
Journal of Analytical Sciences, Methods and Instrumentation (JASMI) , 2013, DOI: 10.4236/jasmi.2013.33A002
Abstract:

A glycoprotein, bovine serum albumin (BSA) was used as a model compound for encapsulation in a sol-gel matrix. Dried gels were ground into powders and meshed to achieve particle sizes less than 250 μm. The products were washed with phosphate buffer. Capillary electrophoresis was used to evaluate the encapsulation efficiency and the kinetic properties of protein release. Several parameters, including the pH and composition of the background electrolyte, were investigated in an effort to eliminate the matrix effect from the determination of release kinetics. Complete separation of the silica matrix from BSA was using phosphate buffer, an applied voltage of 15 kV, and detection at 278 nm. Kinetic studies indicated that most of the BSA was released in the first 5 h. The rate of BSA release gradually decreased, and some BSA after 25 h. These results indicated that dilute potassium phosphate buffer could accelerate protein release, but this was not observed for the concentrations greater than 50 mM. We believe the developed method has potential utility in other systems for in vitro matrix dissolution and drug release studies.

Study of in Vitro Interaction of Sildenafil Citrate with Bovine Serum Albumin by Fluorescence Spectroscopy  [PDF]
Md. Abdus Salam, Md. Rokonujjaman, Asma Rahman, Ummay Nasrin Sultana, Md. Zakir Sultan
Pharmacology & Pharmacy (PP) , 2015, DOI: 10.4236/pp.2015.62012
Abstract: In vitro interaction of sildenafil citrate (SC) with bovine serum albumin (BSA) was investigated at two excitation wavelengths of BSA (280 nm and 293 nm) at two different temperatures (298 K and 308 K) by fluorescence emission spectroscopy. The study showed that quenching of BSA fluores-cence by sildenafil citrate was the result of formation BSA-SC complex with probable involvement of both tryptophan and tyrosine residues of BSA. Fluorescence quenching constant was determined from Stern-Volmer equation, and both static quenching and dynamic quenching were showed for BSA by SC at the conditions. Van’t Hoff equation was used to measure the thermodynamic parameters ΔG, ΔH, and ΔS at the temperatures which indicated that the hydrogen bond and the hydrophobic forces played major roles for BSA-SC complexation. The binding number (n) was found to be ≈1 indicating that one mole BSA bound with one mole SC. The binding affinity of SC to BSA was calculated at different temperatures. The binding constant was decreased with increasing temperatures indicating that stability of BSA-SC complex decreased with increasing temperatures.
A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin  [PDF]
Atanu Singha Roy, Debi Ranjan Tripathy, Angshuman Chatterjee, Swagata Dasgupta
Journal of Biophysical Chemistry (JBPC) , 2010, DOI: 10.4236/jbpc.2010.13017
Abstract: The interaction of naringin with bovine serum albumin has been performed using fluorescence, circular dichroism and fourier transform infrared spectroscopy in 20 mM phosphate buffer of pH 7.0 as well as molecular docking studies. The changes in enthalpy (ΔH°) and entropy (ΔS°) of the interaction were found to be +18.73 kJ/mol and +143.64 J mol-1 K-1 respectively, indicating that the interaction of naringin with bovine serum albumin occurred mainly through hydrophobic interactions. Negative values of free energy change (ΔG°) at different temperatures point toward the spontaneity of the interaction. Circular dichroism studies reveal that the helical content of bovine serum albumin decreased after interaction with naringin. According to the F?rster non-radiative energy transfer theory the distance between Trp 213 residue and naringin was found to be 3.25 nm. Displacement studies suggest that naringin binds to site 1 (subdomain IIA) of bovine serum albumin (BSA) which was also substantiated by molecular docking studies.
BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
ABUIN,E; ASPéE,A; LISSI,E; LEóN,L;
Journal of the Chilean Chemical Society , 2007, DOI: 10.4067/S0717-97072007000200017
Abstract: the association of rose bengal (rb) with bovine serum albumin (bsa) was investigated by absorbance spectroscopy. the binding constant was determined from the effect observed in the absorbance of rb at 548 nm upon addition of the protein according with the benesi-hildebrand treatment. results were obtained in phosphate buffer at ph = 7.0. the effect of the salinity of the buffer and the sensitivity of the binding constant to the presence of urea were also studied. the results obtained allow to conclude that the binding of rb to bsa is dominated by hydrophobic effects
Forma??o de multicamadas de polissacarídeos e proteína
Fujimoto, Juliana;Reis, Eduardo Alexandre de Oliveira;Petri, Denise F. S.;Campana Filho, Sérgio P.;
Química Nova , 2002, DOI: 10.1590/S0100-40422002000500010
Abstract: in this work the formation of multilayers composed by carboxymethylcellulose (cmc), chitosane and bovine serum albumin (bsa) was studied by ellipsometry. first, the adsorption behavior of carboxymethylcellulose onto amino-terminated surfaces was investigated as a function of molecular weight and average degree of substitution of cmc. the influence of these parameters on the adsorbed amount of cmc onto amino-terminated substrates was absent. however, the interaction of cmc covered surfaces with chitosane and bsa was favored when the average degree of substitution of cmc was increased. the adsorption of bsa onto the polysaccharide systems was studied as a function of ph. at the isoelectric point of bsa a maximum in the adsorbed amount was found.
Binding of Dexamethasone Phosphate and Testosterone Phenyl Propionate to Bovine Serum Albumin: Drug?drug Interaction at the Binding Site
M. M. Rahman,A.B.S.M. Osman Gani,M.A. Choudhury,M.H. Rahman
Pakistan Journal of Biological Sciences , 2001,
Abstract: The binding of dexamethasone phosphate (DP) and testosterone phenyl propionate, (TPP) two semisynthetic steroids, to bovine serum albumin (BSA) was studied by equilibrium dialysis method at 25°C and pH 7.4 with a view to have an insight into the competitive binding characteristics of these two drugs, when bound to BSA simultaneously. There was increase in free concentration of DP due to addition of TPP and vice versa during concurrent administration of these two drugs, thereby causing reduced binding of these two drugs to BSA. However, the free fraction was not increased up to a level as it was expected from direct competitive displacement. In absence of the site I specific probe (warfarin sodium), DP after being displaced by TPP or vice versa from its high affinity binding site (site II) rebound to its low affinity binding site (site I) on BSA. However, when the site I was sufficiently blocked by warfarin, the increment in the free concentration of the displaced drug was more prominent. This form of modified displacement has been referred to as site-to-site displacement.
Forma o de multicamadas de polissacarídeos e proteína
Fujimoto Juliana,Reis Eduardo Alexandre de Oliveira,Petri Denise F. S.,Campana Filho Sérgio P.
Química Nova , 2002,
Abstract: In this work the formation of multilayers composed by carboxymethylcellulose (CMC), chitosane and bovine serum albumin (BSA) was studied by ellipsometry. First, the adsorption behavior of carboxymethylcellulose onto amino-terminated surfaces was investigated as a function of molecular weight and average degree of substitution of CMC. The influence of these parameters on the adsorbed amount of CMC onto amino-terminated substrates was absent. However, the interaction of CMC covered surfaces with chitosane and BSA was favored when the average degree of substitution of CMC was increased. The adsorption of BSA onto the polysaccharide systems was studied as a function of pH. At the isoelectric point of BSA a maximum in the adsorbed amount was found.
BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
E ABUIN,A ASPéE,E LISSI,L LEóN
Journal of the Chilean Chemical Society , 2007,
Abstract: The association of Rose Bengal (RB) with bovine serum albumin (BSA) was investigated by absorbance spectroscopy. The binding constant was determined from the effect observed in the absorbance of RB at 548 nm upon addition of the protein according with the Benesi-Hildebrand treatment. Results were obtained in phosphate buffer at pH = 7.0. The effect of the salinity of the buffer and the sensitivity of the binding constant to the presence of urea were also studied. The results obtained allow to conclude that the binding of RB to BSA is dominated by hydrophobic effects
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