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 procedure appears to be a specific and sensitive technique for the localization of serotonin in the central nervous system of the rat and has the advantage that adjacent sections can be examined by the immunofluorescence method using antisera to a variety of antigens.
517 citations
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TL;DR: This paper characterized nanoparticle uptake by endothelial cells in cell culture and demonstrated biocompatability of nanoparticles with the cells, demonstrating that nanoparticles could be used for localizing therapeutic agents or gene into endothelium.
509 citations
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TL;DR: Characterizations and bioactivities show that the conjugate samples indeed contain both carbon nanotubes and BSA proteins and that the protein species are intimately associated with the nanot tubes.
Abstract: Carbon nanotubes are functionalized by bovine serum albumin (BSA) proteins via diimide-activated amidation under ambient conditions. The nanotube-BSA conjugates thus obtained are highly water-soluble, forming dark-colored aqueous solutions. Results from characterizations using atomic force microscopy (AFM), thermal gravimetric analysis, Raman, and gel electrophoresis show that the conjugate samples indeed contain both carbon nanotubes and BSA proteins and that the protein species are intimately associated with the nanotubes. Bioactivities of the nanotube-bound proteins are evaluated using the total protein micro-determination assay (the modified Lowry procedure). The results show that the overwhelming majority (∼90%) of the protein species in the nanotube-BSA conjugates remain bioactive.
507 citations
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TL;DR: Overall, flavonoids display moderate affinities for albumins (binding constants in the range 1-15 x 10(4) M(-1), flavones and flavonols being most tightly bound), and it can be proposed that the binding of flavonol primarily takes place in subdomain IIA.
496 citations
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TL;DR: Glutaraldehyde was found to react with the α-amino groups of amino acids, the N-terminal amino groups of some peptides and the sulfhydryl group of cysteine, and the phenolic and the imidazole rings of tyrosine and histidine derivatives were partially reactive.
491 citations