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.

Study on the interaction of 3,3-bis(4-hydroxy-1-naphthyl)-phthalide with bovine serum albumin by fluorescence spectroscopy

Abstract: The interaction between 3,3-bis(4-hydroxy-1-naphthyl)-phthalide (NPP) and bovine serum albumin (BSA) have been studied by fluorescence spectroscopy. The binding of NPP quenches the BSA fluorescence. By the fluorescence quenching results, it was found that the binding constant K = 5.30 × 10 4 L mol −1 , and number of binding sites n = 0.9267. In addition, according to the synchronous fluorescence spectra of BSA, the results showed that the fluorescence spectra of BSA mainly originate from the tryptophan residues. Finally, the distance between the acceptor NPP and BSA was estimated to be 1.94 nm using Foster's equation on the basis of fluorescence energy transfer. The interaction between NPP and BSA has been verified as consistent with the static quenching procedure and the quenching mechanism is related to the energy transfer.

Mechanism of High Pressure Denaturation of Proteins

Abstract: High pressure denaturation of ovalbumin, bovine serum albumin (BSA) and β-lactoglobulin was assessed by spectrofluorometry, specific rotation analysis and differential scanning calorimetry (DSC), and compared with heat and chemical denaturation. In all cases the denaturation caused by high pressure was similar to that caused by the cleavage of hydrogen bonds with urea or guanidine hydrochloride.

Optical Properties of Thin Layers of Bovine Serum Albumin, γ-Globulin, and Hemoglobin

Abstract: We have used spectroscopic ellipsometry to determine the dielectric functions of thin films of γ-globulin, bovine serum albumin, and hemoglobin in the visible and near-uv photon energy range. We show that both thickness and dielectric function can be resolved for monomolecular films adsorbed on substrates with relatively low polarizability. The data which we consider to be closest to the intrinsic dielectric response of the protein films were obtained on HgTe and HgCdTe substrates. Less resolution was obtained on silicon substrates. For a density-deficient film, we were able to model the dielectric response with effective medium theories, and the void fraction could be determined.

Protein Transport in Nanoporous Membranes Modified with Self-Assembled Monolayers of Functionalized Thiols

Abstract: Control of external pH and ionic strength is used to separate proteins with surface-modified, nanoporous polycarbonate track etched (PCTE) membranes. The porous PCTE membranes were modified with monolayers of self-assembled thiols (HSC10H20COOH) on electroless gold. The hydraulic radius of the pores in the surface-modified membranes was 8.7 nm. Two proteins of nearly identical molecular weight, bovine serum albumin (BSA) and bovine hemoglobin (BHb), were used as the permeants. The fluxes of BSA and BHb through the membranes show maximum values at the isoelectric points (pI) of the proteins. At pH values above and below the pI, charge interactions between the proteins, their counterions, and the pore surface leads to a decrease in flux. The imposition of a difference in ionic strength across the membrane causes osmotic flow and leads to a significant increase in the protein fluxes and an enhancement of the selectivity of BSA over BHb. In protein separation experiments, the BSA and BHb fluxes are nearly 3 t...