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 article, the effects of bovine serum albumin (BSA) on TNFα-induced expression of adhesion molecules in cultured human aortic endothelial cells (HAEC) were investigated.
Abstract: Objective: Leukocyte adhesion to, and transmigration across, the vascular endothelium are critical initiating steps in inflammation and atherosclerosis. We hypothesized that albumin, the major plasma protein, acts as an anti-inflammatory agent towards endothelial cells. Methods and Results: To test the hypothesis, we studied the effects of bovine serum albumin (BSA) on TNFα-induced expression of adhesion molecules in cultured human aortic endothelial cells (HAEC). We found that incubation of HAEC for 16 h with BSA (0.5–5%, w/v) dose-dependently inhibited TNFα-induced mRNA and protein expression of vascular cell adhesion molecule-1 (VCAM-1), but not intercellular adhesion molecule-1 nor E-selectin. Yeast recombinant human serum albumin exerted similar inhibitory effects on VCAM-1 expression, whereas γ-globulin was ineffective. BSA also significantly inhibited TNFα-induced adhesion of monocytic THP-1 cells to HAEC in a dose-dependent manner. Furthermore, BSA strongly inhibited activation and nuclear translocation of the transcription factor, nuclear factor-κB (NF-κB). For example, the physiologically relevant concentration of 5% BSA inhibited NF-κB activation by 90±7%, VCAM-1 mRNA and protein expression by 81±4 and 80±13%, respectively, and THP-1 adhesion by 73±9% ( n = 3). The inhibitory effect of BSA on TNFα-induced VCAM-1 expression was not attenuated by inhibition of intracellular GSH synthesis. Conclusions: Our data show that physiological concentrations of albumin selectively inhibit TNFα-induced upregulation of VCAM-1 expression and monocyte adhesion, most likely by inhibiting NF-κB activation in a GSH-independent manner.
140 citations
TL;DR: A method for the determination of mixed disulfides of proteins and low-molecular-weight peptides and amino acids is described, which appears to differ from mercaptalbumin with respect to the pairing of the disulfide bonds.
140 citations
TL;DR: The specific binding to bovine serum albumin of anionic and non-ionic surfactants with C12 acyl chains has been studied by high sensitivity isothermal titration calorimetry and suggests that binding to low affinity sites exhibits energetic parameters; in particular, a large negative change in heat capacity, which is characteristic of hydrophobic interactions.
140 citations
TL;DR: The Standards Committee of the AACC presents a discussion of the nature of total serum protein and the problems associated with its determination, and proposes that protein be defined as polypeptide material, and that a reference preparation be promulgated for interlaboratory use.
Abstract: The Standards Committee of the AACC presents a discussion of the nature of total serum protein and the problems associated with its determination. Proposals are made that protein be defined as polypeptide material, and that a reference preparation be promulgated for interlaboratory use. The reference material suggested is bovine serum albumin, produced to rigid specifications and distributed as a stable 7% (w/v) solution, the concentration of which has been established by careful dry weight assay. Comments of readers are invited.
140 citations
TL;DR: This synthesis method is a new technique for directly attaching gold nanoparticles to macromolecular proteins and demonstrates that the disulfide bonds in the conjugated protein are broken and thus are available for interaction with the nanoparticle surface.
Abstract: We report the synthesis of gold nanoparticles directly conjugated to bovine serum albumin protein by chemical reduction in aqueous solution. Transmission electron microscopy reveals that the gold nanoparticles are well dispersed with an average diameter less than 2 nm, and elemental analysis verifies the composition of the gold-protein conjugates. Infrared spectroscopy confirms that the polypeptide backbone is not cleaved during the conjugation process and that the side chain functional groups remain intact. Raman spectroscopy demonstrates that the disulfide bonds in the conjugated protein are broken and thus are available for interaction with the nanoparticle surface. This synthesis method is a new technique for directly attaching gold nanoparticles to macromolecular proteins.
140 citations