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: CDP‐diglyceride is converted to phosphatidyl inositol by several particulate subcellular fractions of guinea pig brain, with highest specific activity in the microsomal fraction.
Abstract: —
CDP-diglyceride is converted to phosphatidyl inositol by several particulate subcellular fractions of guinea pig brain, with highest specific activity in the microsomal fraction. Optimal conditions with respect to pH, metal ion concentration, and substrate concentrations have been determined. The reaction was stimulated by the addition of bovine serum albumin and by Tween 80.
Of several dl-CDP-diglycerides synthesized and used as substrates in a spectrophoto-metric assay for the enzyme, dl-CDP-didecanoin was the most active.
The enzyme showed a high selectivity for myo-inositol. Of a number of compounds tested, only scyllo-inosose and epi-inosose served as substrates. Three inositol isomers and three myo-inositol monophosphates inhibited the reaction slightly. The most potent inhibitor found was galactinol, a myo-inositol galactoside.
124 citations
TL;DR: The results of the research show that the as-prepared Ag2S nanorods are monodispersed with sizes about 40 nm in diameter and 220 nm in length, and exhibit a high degree of crystallinity and good photoluminescence.
Abstract: Highly ordered silver sulfide nanorods conjugated with the Bovine Serum Albumin (BSA) protein have been successfully achieved at ambient temperature. Such a process is very simple and controllable, directly using silver nitrate and thioacetamide (TAA) as the reactants in the aqueous solution of BSA. The products have been characterized by XRD, HRTEM-SAED, SEM-EDS, TG-DTA, FT-IR, and CD spectroscopy. The results of the research show that the as-prepared Ag2S nanorods are monodispersed with sizes about 40 nm in diameter and 220 nm in length, and exhibit a high degree of crystallinity and good photoluminescence. Furthermore, an interesting mechanism is discussed for the formation of the Ag2S nanorods.
124 citations
TL;DR: High-performance separation of proteins, based on immobilized different metals on the column, were described and the influence of pH on the adsorption capacity of bovine serum albumin on the Cu2+-IDA continuous rod column was investigated.
124 citations
TL;DR: This blocking ELISA is superior to a commercially available indirect ELISA and to the 24-h virus neutralization test in detecting low antibody levels in serum and is able to detect specific antibodies in serum as early as 7 days postinfection.
Abstract: By using a monoclonal antibody directed against an epitope located on glycoprotein B of bovine herpesvirus 1 (BHV1), a simple, convenient blocking enzyme-linked immunosorbent assay (ELISA) which combines a high sensitivity with a low false-positive rate has been developed. The test can be performed at low variance on undiluted bovine serum samples. The epitope on glycoprotein B appears to be conserved, because it could be detected by immunostaining in all of 160 BHV1 isolates originating from 10 countries. In testing 215 anti-BHV1 antibody-negative and 179 anti-BHV1 antibody-positive serum samples, specificity and sensitivity were 0.96 and 0.99, respectively. This blocking ELISA is superior to a commercially available indirect ELISA and to the 24-h virus neutralization test in detecting low antibody levels in serum. In addition, this blocking ELISA is able to detect specific antibodies in serum as early as 7 days postinfection. To minimize any risk of introducing latent BHV1 carriers among noninfected cattle, this blocking ELISA would be, in our opinion, the test of choice.
124 citations
TL;DR: In this article, a quasi-elastic light scattering (QELS) and electrophoretic light scattering in dilute electrolyte solution was used to study the interaction between globular proteins and a number of synthetic polyelectrolytes.
Abstract: Complexation between globular proteins (bovine serum albumin, bovine pancreas ribonuclease, and chicken egg lysozyme) and a number of synthetic polyelectrolytes was studied by quasi-elastic light scattering (QELS) and electrophoretic light scattering in dilute electrolyte solution. For each polyion-protein pair, there is a well-defined critical pH at which binding commences (pH,). At this pH, QELS reveals fast and slow diffusion modes corresponding to free protein and complex, respectively; the relative amplitude of the latter increases with pH in the case of polycations, with opposite pH dependence for polyanions. Further pH change produces phase separation at a second well-defined point (pH+). The electrophoretic mobility of the polymer begins to change at pH, and moves toward zero as pH approaches pH+. These results are discussed in terms of (1) the role of protein “charge patches” as binding sites and (2) the alternative possibilities of intra- and inter-polyion
123 citations