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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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Journal ArticleDOI
TL;DR: The results clearly demonstrate that the visible-light form of the surfactant causes a greater degree of protein unfolding than the UV- light form, providing a means to control protein folding with light that, within the resolution of SANS, appears to be completely reversible.
Abstract: The photoresponsive interaction of light-sensitive azobenzene surfactants with bovine serum albumin (BSA) at neutral pH has been investigated as a means to control protein folding with light irradiation. The cationic azobenzene surfactant undergoes a reversible photoisomerization upon exposure to the appropriate wavelength of light, with the visible-light (trans) form of the surfactant being more hydrophobic than the UV-light (cis) form. As a consequence, the trans form exhibits enhanced interaction with the protein compared to the cis form of the surfactant, allowing photoreversible control of the protein folding/unfolding phenomena. Small-angle neutron-scattering (SANS) measurements are used to provide detailed information on the protein conformation in solution. A fitting of the protein shape to a low-resolution triaxial ellipsoid model indicates that three discrete forms of the protein exist in solution depending on the surfactant concentration, with lengths of approximately 90, 150, and 250 A, respec...

115 citations

Journal ArticleDOI
TL;DR: In this paper, the surface-enhanced Raman spectra of water-soluble proteins (lysozyme and bovine serum albumin), dipeptides and amino acids were analysed.
Abstract: Surface-enhanced Raman (SER) spectra of water-soluble proteins (lysozyme and bovine serum albumin), dipeptides and amino acids were analysed. Chemisorption is a necessary condition for the appearance of SER spectra on silver electrodes and hydrosols for these compounds. The Raman cross-section enhancement per molecule may reach a factor of 105–106, depending closely on the frequency of the vibration band considered. The mechanism of enhancement has a short-range character and is attributed to the π-electron complexes of the aromatic amino acids side-chains and σ-complexes of the molecular groups containing unshared electron pairs with the metal. The effect of induced optical activity in the visible region for aromatic amino adsorbed by silver hydrosols has been elucidated.

115 citations

Journal ArticleDOI
TL;DR: It is suggested that considerable care is needed to ensure that accurate and reproducible results are obtained from studies quantifying this peptide, as well as factors influencing the recovery and measurement of AM in the assay.
Abstract: We describe a specific and sensitive RIA for human adrenomedullin (AM)(1–52). The detection limit and the concentration required for 50% inhibition of binding were 0.1 and 1.2 fmol/tube, respectively. Cross-reactivities with AM(1–12), AM(13–52), calcitonin gene-related peptide, amylin, and other vasoactive hormones were negligible. AM immunoreactivity in normal subjects ranged from 2.7 to 10.1 pmol/L (n = 44). We investigated factors influencing the recovery and measurement of AM in the assay. Recovery of labeled AM (>80%) was markedly higher than that of unlabeled AM (56%). Immunoreactivity of exogenous AM added to plasma decreased up to 70% over four freeze–thaw cycles, whereas endogenous AM was stable. Alkali-treated casein (1 g/L) reduced adsorption of AM to surfaces and significantly increased assay precision compared with bovine serum albumin ( P <0.0001). HPLC separation of extracted plasma verified the presence of AM(1–52). We suggest that considerable care is needed to ensure that accurate and reproducible results are obtained from studies quantifying this peptide.

115 citations

Journal ArticleDOI
TL;DR: In this article, the effects of phytate and partially hydrolyzed sodium phytates on pepsin digestion of casein and bovine serum albumin were evaluated by an in vitro procedure using dialy-sates.
Abstract: The effects of sodium phytate and partially hydrolyzed sodium phytate (0 - 82% hydrolyzed) on pepsin digestion of casein and bovine serum albumin were evaluated by an in vitro procedure using dialy-sates of pepsin digestion over a period of 0 – 23 hr. The inhibitory effect of phytate differed with substrate and increased with dose level. At the highest phytate level, the digestion of casein and bovine serum albumin was reduced by 14% and 7%, respectively. The inhibitory effect of the phytate was inversely correlated with the degree of phytate hydrolysis. Hydrolysis for 16 hr almost eleminated the inhibitory effect of phytate.

114 citations

Journal ArticleDOI
TL;DR: It is suggested that SPP or an SPP-like protein contributes to the neuronal survival-promoting activity of serum and is supported more effectively than inorganic selenium.
Abstract: We purified from bovine serum a glycoprotein that promotes the survival of rat embryonic neurons cultured from septum and other brain regions. A 40,000-fold purification was achieved by using a combination of ammonium sulfate precipitation, Zn 2+ affinity chromatography, Cibacron blue 3-GA dye affinity chromatography, ABx ion exchange chromatography, and preparative PAGE. The active protein had an apparent molecular weight of 50–60 kDa. The concentration required for half-maximal survival (EC 50 ) was 12 ng/ml (∼200 pm) for the final fraction. Amino acid sequencing after cyanogen bromide cleavage yielded two sequences that are homologous to regions of deduced sequence of the selenoprotein-P (SPP) family in bovine, rat, and human. Antibodies against a synthetic peptide within the bovine SPP sequence immunoprecipitated and inhibited the survival-promoting activity of a partially purified serum fraction. The purified protein supported neuronal survival more effectively than inorganic selenium. These results suggest that SPP or an SPP-like protein contributes to the neuronal survival-promoting activity of serum.

114 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023475
2022983
2021423
2020460
2019468
2018489