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: For the H3-subtype virus A/Memphis/1/71 x A/Bel/42 (H3N1), sensitivity to beta inhibitors was determined by the oligosaccharide at residue 165 of the hemagglutinin, this glycosylation site being lost in a resistant mutant selected by growth in the presence of bovine serum as discussed by the authors.
Abstract: Normal bovine and mouse sera contain a component, termed beta inhibitor, that inhibits the infectivity and hemagglutinating activity of influenza A viruses of the H1 and H3 subtypes. We have previously shown these beta inhibitors to be mannose-binding lectins that apparently act by binding to carbohydrate on the viral hemagglutinin, blocking access of the receptor-binding site to receptors on host cells (E. M. Anders, C. A. Hartley, and D. C. Jackson, Proc. Natl. Acad. Sci. USA 87:4485-4489, 1990). For the H3-subtype virus A/Memphis/1/71 x A/Bel/42 (H3N1), sensitivity to beta inhibitors is determined by the oligosaccharide at residue 165 of the hemagglutinin, this glycosylation site being lost in a resistant mutant selected by growth in the presence of bovine serum. In the present study, we sequenced the hemagglutinin genes of additional bovine serum-resistant mutants derived from influenza viruses A/Philippines/2/82 (H3N2) and A/Brazil/11/78 (H1N1). The results confirm the importance of carbohydrate at residue 165 for inhibitor sensitivity of H3 viruses and implicate carbohydrate at residue 87 (94a in the H3 numbering system) as an important determinant in the sensitivity of H1-subtype viruses to the bovine inhibitor. Unlike the two H3 mutants, which had also gained resistance to hemagglutination inhibition by mouse serum, the H1 bovine serum-resistant mutant remained sensitive to the mouse beta inhibitor, suggesting that inhibition by the two types of sera is mediated by distinct mannose-binding lectins. In support of this hypothesis, the beta inhibitors in bovine and mouse sera were shown to differ in their pattern of inhibition by monosaccharides and in their sensitivity to 2-mercaptoethanol. In these and other properties, the bovine inhibitor closely resembled conglutinin, a Ca(2+)-dependent N-acetylglucosamine- and mannose-binding lectin present in bovine serum but absent from the serum of other species. Furthermore, polyclonal and monoclonal anticonglutinin antibodies abrogated the hemagglutination-inhibiting activity of bovine serum. Direct binding of conglutinin to the parent viruses and reduced binding to their respective mutants were confirmed by radioimmunoassay.
113 citations
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TL;DR: Binary patterned peptides are suitable for biosensing directly in complex biological matrixes in SPR biosensing with a detection limit of 1-10 pM in PBS, similar to other optical or electrochemical techniques.
Abstract: Near-zero fouling monolayers based on binary patterned peptides allow low nanomolar detection of the matrix metalloproteinase-3 (MMP-3) directly in crude bovine serum, without sample pretreatment, ...
113 citations
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112 citations
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TL;DR: The results clearly demonstrate that nominal and relative toxic potencies of organochlorine pesticides and chlorophenols determined in vitro are substantially influenced by effects of protein binding on availability.
112 citations
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TL;DR: The results suggest that at low concentrations, warfarin binds at the high-affinity sites (HAS), while low-Affinity binding sites (LAS) are occupied at higher concentrations.
112 citations