Topic
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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TL;DR: In this paper, the proteins in the serum obtained after removal of the denatured serum proteins with the casein at pH 4.6 were examined by a quantitative electrophoretic procedure.
151 citations
TL;DR: The results suggest that the low adhesiveness of BHK cells and leucocytes on plain polystyrene in sera-containing media is due both to the low binding of fibronectin and to the binding of serum albumin, alpha-1-antitrypsin and alpha-2-macroglobulin.
Abstract: Binding curves for the adsorption of plasma fibronectin, alpha-1-antitrypsin, alpha-2-macroglobulin, ceruloplasmin, transferrin and bovine serum albumin to plain and to hydroxylated polystyrene surfaces were measured. These curves were correlated with the adhesion of BHK cells and leucocytes to these adsorbed protein surfaces in protein-free culture media. Hydroxylated polystyrene adsorbed less of alpha-1-antitrypsin, alpha-2-macroglobulin and albumin than the plain polystyrene. On the other hand the hydroxylated surfaces bound more fibronectin than the plain polystyrene surfaces. Hydroxylated polystyrene surfaces were also more adhesive for both BHK cells and leucocytes than plain polystyrene: a result confirming earlier work. The competition of fibronectin for adsorption to plain polystyrene with alpha-1-antitrypsin, alpha-2-macroglobulin and ceruloplasmin was measured and correlated with effects on cell adhesion. The results suggest that the low adhesiveness of BHK cells and leucocytes on plain polystyrene in sera-containing media is due both to the low binding of fibronectin and to the binding of serum albumin, alpha-1-antitrypsin and alpha-2-macroglobulin. The relative unimportance of fibronectin in adhesion to these surfaces is shown by the finding that cell attachment will not occur to polystyrene surfaces that have bound high levels of the antiadhesive proteins in the presence of fibronectin, even though attachment will occur in the absence of fibronectin provided that the antiadhesive proteins are lacking.
151 citations
TL;DR: The mechanism of aggregation of bovine serum albumin (BSA) by poly(allylamine) hydrochloride (PAH) is investigated as a function of the mixing ratio r defined as the ratio of the number of BSA molecules and PAH chains present in the solution, under pH conditions of strong binding between the two partners.
Abstract: The mechanism of aggregation of bovine serum albumin (BSA) by poly(allylamine) hydrochloride (PAH) is investigated as a function of the mixing ratio r defined as the ratio of the number of BSA molecules and PAH chains present in the solution, under pH conditions of strong binding between the two partners. It is found that as r increases the turbidity first increases, passes through a maximum at a value rmax before decreasing again. For small and large values of r, one forms small aggregates in the 10 nanometer size range, whereas at rmax, the size of the aggregates becomes of the order of micrometers. The structure of the aggregates appears to be independent of the history of the systems but depends only on the value of r despite the strong BSA/PAH binding. The desaggregation of the large aggregates formed at rmax by the addition of BSA or PAH is shown to be an isenthalpic process and is thus entirely entropically driven. Moreover, we prove that rmax corresponds to the state of the system where both the P...
150 citations
TL;DR: DT diaphorase was purified to homogeneity from rat liver and characterized and it was demonstrated that bovine serum albumin competes with the native enzyme for K3 and dicumarol, probably through the ability of this simple protein to associate with these substances, preventing the formation of enzyme-K3 and enzyme-dicumarl complexes, and leading to the apparent increase in enzyme activity.
150 citations
15 Apr 2009
TL;DR: The experimental results demonstrate that the intermolecular chain associations were formed between alginate chains and protein molecules in either the native form or the heat pre-denatured form, mainly driven by the electrostatic interactions between the oppositely charged amino acids and the anionic polysaccharide macromolecules.
Abstract: The intermolecular interactions between the model protein, bovine serum albumin (BSA) and a biocompatible polysaccharide, sodium alginate, have been investigated. Both the native BSA and the heat pre-denatured BSA were utilized to study, in parallel, the effect of protein conformational change during the protein-alginate complex formation. In this work, a comparison was performed between the native BSA and the heat-denatured BSA incubated sodium alginate mixtures by using zeta potential analyzer, dynamic light scattering (DLS) and turbidimetric analysis of the systems in combination with protein conformational tools, Fourier transform infrared spectroscopy (FT-IR) and size exclusion chromatography (SE-HPLC). The experimental results demonstrate that the intermolecular chain associations were formed between alginate chains and protein molecules in either the native form or the heat pre-denatured form, mainly driven by the electrostatic interactions between the oppositely charged amino acids and the anionic polysaccharide macromolecules. However, the majority of BSA was recovered from the dissociation of protein-alginate complexes and maintained its secondary structure and conformational property. Therefore, alginate is promising as a bioactive compound carrier.
150 citations