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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113 citations
TL;DR: The studies suggest that albumin has adequate binding capacity for the low plasma levels of V LCFA with 20 to 26 carbons, but the protein may not be able to bind longer chain VLCFA.
113 citations
TL;DR: Far UV circular dichroism and fluorescence spectroscopy were used to investigate the interaction between bovine serum albumin (BSA) and metallothionein (MT) and a decrease in KSV values were observed which indicates conformational changes in BSA upon binding MT.
Abstract: Far UV circular dichroism (CD) and fluorescence spectroscopy were used to investigate the interaction between bovine serum albumin (BSA) and metallothionein (MT). Both spectroscopic probes gave proofs on the interaction of the two proteins. At pH 4.0, 7.0 and 9.0, BSA showed a negative increase in ellipticity at the far-UV range in the presence of MT indicating an increase in α-helical content and a decrease in β-sheet structure. In the presence of MT at pH 4.0 and 9.0, a decrease in fluorescence intensity was observed. Tryptophan fluorescence quenching experiments were also performed using acrylamide and KI as quenchers. Under acidic conditions, a four-fold increase in Stern-Volmer constant (KSV) was observed for BSA + MT. At neutral and basic conditions, a decrease in KSV values were observed which indicates conformational changes in BSA upon binding MT. These changes are close to the region where the tryptophan residues are located in the protein.
113 citations
TL;DR: The role of surface hydrophobicity in the surface properties of proteins was investigated in this paper, where changes in the emulsifying and foaming properties of ovalbumin, 7S globulin, κ-casein, β-lactoglobuHn and bovine serum albumin were followed during heat denaturation.
Abstract: Changes in the emulsifying and foaming properties of ovalbumin, 7S globulin, κ-casein, β-lactoglobuHn and bovine serum albumin were followed during heat denaturation, and these surface properties were correlated with the corresponding surface hydrophobicity, in order to investigate the role of surface hydrophobicity in the surface properties of proteins. The surface hydrophobicity of ovalbumin, 7S globulin and jc-casein increased with heat denaturation, while that of β-lactoglobuHn and bovine serum albumin decreased. The emulsifying activity and emulsion stability of proteins correlated linearly with surface hydrophobicity, although protein structure changed greatly during heat denaturation. On the other hand, the foaming power of proteins correlated curvilinearly with surface hydrophobicity during heat denaturation. No significant correlation was observed between the foam stability and the surface hydrophobicity of proteins.On the basis of these results, the relationships between the surface properties a...
113 citations
TL;DR: It is concluded that the dextran-grafted branched PEI improved the stability of the DNA-polymer complexes and showed potential to conjugate with ligands for in vivo targeted gene delivery.
113 citations