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Bovine serum albumin

About: Bovine serum albumin is a research topic. Over the lifetime, 19981 publications have been published within this topic receiving 571291 citations. The topic is also known as: BSA.


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Journal ArticleDOI
TL;DR: The greater degree of fluorescence enhancement, the greater stability ofretinol in RBP and PA-RBP to spontaneous degradation at room temperature, the relative resistance to extraction of the bound retinol by ether, and the complete unavailability of the retinols inRBP andPA-R BP for oxidation by liver alcohol dehydrogenase were interpreted as indicating that retinOL is bound with greater affinity to the natural carrier protein than it is to bovine serum albumin or

234 citations

Journal ArticleDOI
TL;DR: In this paper, the correlation between protein solubility and the preferential interactions of proteins with solvent components was critically examined with aqueous MgCl2 as the solvent system, and it was shown that the nature of interactions between proteins and solvent components is the same in solution and in the solid state, which implies no change in protein structure during precipitation.
Abstract: The correlation between protein solubility and the preferential interactions of proteins with solvent components was critically examined with aqueous MgCl2 as the solvent system. Preferential interaction and solubility measurements with three proteins, beta-lactoglobulin, bovine serum albumin, and lysozyme, resulted in similar patterns of interaction. At acid pH (pH 2-3) and lower salt concentrations (less than 2 M), the proteins were preferentially hydrated, while at higher salt concentrations, the interaction was either that of preferential salt binding or low salt exclusion. At pH 4.5-5, all three proteins exhibited either very low preferential hydration or preferential binding of MgCl2. These results were analyzed in terms of the balance between salt binding and salt exclusion attributed to the increase in the surface tension of water by salts, which is invariant with conditions. It was shown that the increase in salt binding at high salt concentration is a reflection of mass action, while its decrease at acid pH is due to the electrostatic repulsion between Mg2+ ions and the high net positive charge on the protein. The preferential interaction pattern was paralleled by the variation of protein solubility with solvent conditions. Calculation of the transfer free energies from water to the salt solutions for proteins in solution and in the precipitate showed dependencies on salt concentration. This indicates that the nature of interactions between proteins and solvent components is the same in solution and in the solid state, which implies no change in protein structure during precipitation. Analysis of the transfer free energies and preferential interaction parameter in terms of the salting-in, salting-out, and weak ion binding contributions has led to the conclusions that, when the weak ion binding contribution is small, the predominant protein-salt interaction must be that of preferential salt exclusion most probably caused by the increase of the surface tension of water by addition of the salt. A necessary consequence of this is salting-out of the protein, if the protein structure is to remain unaltered.

233 citations

Journal ArticleDOI
TL;DR: Initial cell adhesion on self-assembled monolayers (SAMs) of alkanethiols carrying different functional groups including methyl (CH3), hydroxyl (OH), carboxylic acid (COOH), and amine (NH2) is investigated.
Abstract: We investigated initial cell adhesion on self-assembled monolayers (SAMs) of alkanethiols carrying different functional groups including methyl (CH3), hydroxyl (OH), carboxylic acid (COOH), and amine (NH2). The combination of a surface plasmon resonance (SPR) instrument and a total internal reflection fluorescence microscope (TIRFM) allowed us to examine the kinetics of protein adsorption and correlating cell adhesion. Upon exposure of the SAM surface to a serum-containing medium, serum proteins rapidly adsorbed, and cells subsequently approached the surface. Adhesion of human umbilical vein endothelial cells (HUVECs) was greatly affected by surface functional groups; HUVECs adhered well to COOH– and NH2–SAMs, whereas poorly to CH3– and OH–SAMs. The amount of adsorbed protein from the serum-containing medium varied slightly with the terminal groups of the SAMs. On COOH– and NH2–SAMs, HUVECs adhered to bovine serum albumin (BSA)-preadsorbed surfaces with a few minutes delay, suggesting that displacement of preadsorbed BSA with cell-adhesive proteins, such as fibronectin or vitronectin, supports cell adhesion to these surfaces. Since the concentration of cell-adhesive proteins is much less than that of non-adhesive proteins such as BSA, displacement of adsorbed proteins with cell-adhesive proteins plays an important role in initial cell adhesion.

233 citations

Journal ArticleDOI
22 Apr 2013-ACS Nano
TL;DR: This work shows for the first time solid state nanopore measurements of mammalian prion protein, which in its abnormal form is associated with transmissible spongiform encephalopathies, and provides a basis for protein characterization and the study of protein conformational diseases by nanopore detection.
Abstract: Nanopores can be used to detect and analyze single molecules in solution. We have used glass nanopores made by laser-assisted capillary-pulling, as a high-throughput and low cost method, to detect a range of label-free proteins: lysozyme, avidin, IgG, β-lactoglobulin, ovalbumin, bovine serum albumin (BSA), and β-galactosidase in solution. Furthermore, we show for the first time solid state nanopore measurements of mammalian prion protein, which in its abnormal form is associated with transmissible spongiform encephalopathies. Our approach provides a basis for protein characterization and the study of protein conformational diseases by nanopore detection.

232 citations

Journal ArticleDOI
TL;DR: Radiolysis of bovine serum albumin under aerobic and anaerobic conditions was studied by SDS-polyacrylamide gel electrophoresis and the radiation-induced broadening of the serumalbumin peak is interpreted as being a result of intramolecular disulfide exchange.
Abstract: Radiolysis of bovine serum albumin under aerobic and anaerobic conditions was studied by SDS-polyacrylamide gel electrophoresis. After Coomassie Blue or Fast Green staining quantitative evaluations give information about the degradation processes of the protein. Under nitrogen the main reaction is the aggregation caused by covalent cross-links, which includes only a small portion of intermolecular S-S bridges. Under air the radiolysis leads to peptide chain scission, which is not a random process, but yields specific protein fragments. A mechanism for this fragmentation reaction is suggested. The radiation-induced broadening of the serum albumin peak is interpreted as being a result of intramolecular disulfide exchange. In contrast to lactate dehydrogenase the degradation of serum albumin is enhanced by oxygen, probably because of its low tryptophan content.

232 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023475
2022983
2021423
2020460
2019468
2018489