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: The conclusion that human gastric lipase shows no intrinsic specificity for short-chain triacylglycerols and that its apparent specificity is modulated by pH and presence of amphiphile in the incubation medium supports the view that, in the human, gastriclipolysis may play an important role in long-chain fat digestion.
220 citations
TL;DR: The purpose of these measurements was to study the correlation between the three-dimensional organization of BSA native protein structure and its thermodynamic stability and to clarify the non-covalent interactions between the globular proteins and amphipathic molecules.
220 citations
TL;DR: The interaction between bovine serum albumin (BSA) and several surfactants has been investigated by light scattering as discussed by the authors, showing that cooperative binding of DTAB occurs at higher surfactant concentrations than in comparative solutions of SDS and C12E8.
Abstract: The interaction between bovine serum albumin (BSA) and several surfactants has been investigated by light scattering. Anionic (sodium dodecyl sulfate, SDS), cationic (dodecyl trimethylammonium bromide, DTAB), and nonionic (polyoxyethylene 8 lauryl ether, C12E8) surfactants, all containing a C12 alkyl chain, were used to study the effect of different headgroups on the complex formation. The hydrodynamic radii of the complexes obtained by dynamic light scattering indicate that cooperative binding of DTAB occurs at higher surfactant concentrations than in comparative solutions of SDS and C12E8. The effect of chain length is shown for the cationic surfactants DTAB and cetyl trimethylammonium bromide (CTAB, C16 alkyl chain). The higher surface activity of CTAB results in complex formation at a lower surfactant concentration compared to DTAB. The hydrodynamic radii of the BSA−SDS and BSA−DTAB complexes at saturation were determined as ∼5.9 nm and ∼4.8 nm, respectively. The hydrodynamic radius of the reduced BSA...
220 citations
TL;DR: In this article, the relationship of adsorbed layer structure to emulsion stability is discussed, with reference to macroscopic oil-water interfaces and protein-stabilized oil-in-water emulsions.
219 citations
TL;DR: The results indicate that rat liver contains at least two novel and distinct proteins that recognize AGE-modified macromolecules, although p90 may be related to the previously described 90-kD AGE receptor isolated from RAW 264.7 cells.
Abstract: Advanced glycosylation endproducts (AGEs), the glucose-derived adducts that form nonenzymatically and accumulate on tissue proteins, are implicated in many chronic complications associated with diabetes and aging. We have previously described a monocyte/macrophage surface receptor system thought to coordinate AGE protein removal and tissue remodeling, and purified a corresponding 90-kD AGE-binding protein from the murine RAW 264.7 cell line. To identify AGE-binding proteins in normal animals, the tissue distribution of 125I-AGE rat serum albumin taken up from the blood was determined in rats in vivo. These uptake studies demonstrated that the liver was a major site of AGE protein sequestration. Using a solid-phase assay system involving the immobilization of solubilized membrane proteins onto nitrocellulose to monitor binding activity, and several purification steps including affinity chromatography over an AGE bovine serum albumin matrix, two rat liver membrane proteins were isolated that specifically bound AGEs, one migrating at 60 kD (p60) and the other at 90 kD (p90) on SDS-PAGE. NH2-terminal sequence analysis revealed no significant homology between these two proteins nor to any molecules available in sequence databases. Flow cytometric analyses using avian antibodies to purified rat p60 and p90 demonstrated that both proteins are present on rat monocytes and macrophages. Competition studies revealed no crossreactivity between the two antisera; anti-p60 and anti-p90 antisera prevented AGE-protein binding to rat macrophages when added alone or in combination. These results indicate that rat liver contains at least two novel and distinct proteins that recognize AGE-modified macromolecules, although p90 may be related to the previously described 90-kD AGE receptor isolated from RAW 264.7 cells. The constitutive expression of AGE-binding proteins on rat monocytes and macrophages, and the sequestration of circulating AGE-modified proteins by the liver, provides further evidence in support of a role for these molecules in the normal removal of proteins marked as senescent by accumulated glucose-derived covalent addition products, or AGEs.
219 citations