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 results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed, and the quenching mechanism of fluorescence of BSA by monoammonium glycyrrhizinate was discussed.
586 citations
TL;DR: Perfluorooctane sulfonic acid in serum is in general bound to albumins, and it is unlikely that PFOS would cause displacement of hormones from serum proteins in wildlife.
Abstract: Perfluorooctane sulfonic acid (PFOS) accumulates in the liver and blood of exposed organisms. The potential for these surfactant molecules to interfere with hormone/protein interactions in blood is of concern given the importance of these interactions. The PFOS binding to serum proteins was investigated by assessing its ability to displace a variety of steroid hormones from specific binding proteins in the serum of birds and fishes. Perfluorooctane sulfonic acid had only a weak ability to displace estrogen or testosterone from carp serum steroid binding proteins. Displacement of cortisone in avian sera occurred at relatively low PFOS concentrations. Corticosterone displacement potency increased with chain length, and sulfonic acids were more potent than carboxylic acids. The PFOS concentrations estimated to cause these effects were 320 μM or greater, equivalent to serum concentrations greater than 160 mg/L. Using mass spectrometry and direct in vitro binding assays, PFOS was demonstrated to bind strongly to bovine serum albumin (BSA) in a 1:1 stoichiometric ratio. It appears that PFOS in serum is in general bound to albumins. Concentrations of PFOS required to saturate albumin would be in excess of 50 to 100 mg/L. Based on current environmental concentrations, it is unlikely that PFOS would cause displacement of hormones from serum proteins in wildlife.
558 citations
TL;DR: A modification of the Lowry procedure for the rapid and reliable analysis of proteolipid protein involves the addition of sodium dodecyl sulfate to dissolve the lipid-containing protein samples or to maintain the water-soluble apoprotein in solution.
555 citations
TL;DR: An improved cyclic AMP assay using a purified and activated binding protein from bovine skeletal muscle is described, demonstrating that the assay has a remarkable freedom from non-specific interference by materials normally found in crude biological extracts.
553 citations
TL;DR: It turned out that bovine serum albumin (BSA) is composed of 583 amino acid residues, and that its average molecular weight is not 66267.1, and it is corrected to 66430.3.
551 citations