Relevant bibliographies by topics / Bovine serum albumin

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Bovine serum albumin'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Bovine serum albumin"

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&NA;. "Bovine serum albumin." Reactions Weekly &NA;, no. 399 (May 1992): 5. http://dx.doi.org/10.2165/00128415-199203990-00012.

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&NA;. "Bovine serum albumin." Reactions Weekly &NA;, no. 903 (May 2002): 6–7. http://dx.doi.org/10.2165/00128415-200209030-00016.

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Kalchev, Karamfil, Iva Hristova, Gergana Manova, and Lyubomir Manov. "Interaction of the birch-bark terpenoids with human and bovine serum albumins." Acta Scientifica Naturalis 9, no. 3 (November 1, 2022): 25–35. http://dx.doi.org/10.2478/asn-2022-0019.

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Abstract Interactions between pentacyclic triterpenes isolated from white birch (Betula pendula Roth.) bark samples from Northeast Bulgaria and bovine serum albumin or human serum albumin were investigated using fluorescence techniques. The experimental results show the formation of complexes between the isolated triterpenes with serum albumins. Quenching of the intrinsic fluorescence of human serum albumins was monitored by emission spectra of varied quencher concentration solutions. By analysing the fluorescence spectra and fluorescence intensity, some parameters of the serum albumins - quencher interaction were determined to evaluate the type of quenching. An extract containing the isolated triterpenes formed complexes with both bovine serum albumin and human serum albumin, leading to quenching the fluorescence of both albumins by a combined quenching mechanism.
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Maruthamuthu, Meenakshi, and S. Kishore. "Binding of naproxen to bovine serum albumin and tryptophan-modified bovine serum albumin." Proceedings / Indian Academy of Sciences 99, no. 4 (October 1987): 273–79. http://dx.doi.org/10.1007/bf02881249.

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Zhou, Jing Ling, Chun Shu Zhai, Su Yun Yang, Shu Qian Wu, Guo Qing Wu, and Hai Li Xu. "The Friction and Wear of Silicon Nitride Ceramic with BSA Lubricant." Key Engineering Materials 642 (April 2015): 125–29. http://dx.doi.org/10.4028/www.scientific.net/kem.642.125.

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To research the friction and wear of silicon nitride ceramic with bovine serum albumin lubricant, the tribological properties of silicon nitride ceramic against stainless steel were investigated on CETR UMT-2 under lubrication of bovine serum albumin, deionized water, physiological saline and physiological saline mixed with bovine serum albumin. The worn surfaces of silicon nitride ceramic ball and stainless steel pin were examined with a digital microscope (VHX-2000). The friction coefficients of steady state are 0.26, 0.35, 0.69 and 0.8 under bovine serum albumin, physiological saline mixed with bovine serum albumin, physiological saline and deionized water. The lowest friction coefficient of steady state is 0.26 which is under lubrication of bovine serum albumin. The highest friction coefficient is 0.8 under the lubrication of deionized water. The measured worn areas of silicon nitride ceramic balls are 1282.3μm2, 1898.6μm2, 2753.9μm2 and 3645.7μm2 under bovine serum albumin, physiological saline mixed with bovine serum albumin, physiological saline and deionized water. The smallest worn area of silicon nitride ceramic ball is 1282.3μm2 which is measured under the lubrication of bovine serum albumin. The highest worn area of silicon nitride ceramic ball is 3645.7μm2 which was measured under the lubrication of deionized water. The same wear mechanism of silicon nitride ceramic ball had been found under the lubrication of bovine serum albumin, deionized water, physiological saline and physiological saline mixed with bovine serum albumin. The depth of scratches of worn surface of silicon nitride ceramic ball lubricated with BSA is 3μm which are the shallowest.
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Lemli, Beáta, Diána Derdák, Péter Laczay, Dorottya Kovács, and Sándor Kunsági-Máté. "Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin." Molecules 23, no. 8 (July 31, 2018): 1915. http://dx.doi.org/10.3390/molecules23081915.

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Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated by both spectroscopic (UV-vis, Photoluminescence) and calorimetric methods. The interaction was determined on the basis of quenching of albumin by tilmicosin. Results confirm noncovalent binding of tilmicosin on bovine serum albumin with 1:1 stoichiometry associated with pK = 4.5, highlighting possible removal of tilmicosin molecules from the albumin surface through exchange reactions by known competitor molecules. Calorimetric measurements have confirmed the weak interaction between tilmicosin and albumin and reflect enhanced denaturation of the albumin in the presence of tilmicosin antibiotic. This process is associated with the decreased activation energy of conformational transition of the albumin. It opens a new, very quick reaction pathway without any significant effect on the product by noncovalent binding the tilmicosin molecules to the protein molecules. Results highlight the medical importance of these investigations by considerable docking of the selected antibiotic molecules on serum albumins. Although the binding may cause toxic effects in living bodies, the strength of the binding is weak enough to find competitor molecules for effective removals from their surface.
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Liang, Yan Qiu, and Ying Zhang. "Interaction of 4-Nitroaniline with Serum Albumin." Applied Mechanics and Materials 522-524 (February 2014): 337–40. http://dx.doi.org/10.4028/www.scientific.net/amm.522-524.337.

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Bovine serum albumin (BSA) and human serum albumin (HSA) interaction with 4-nitroaniline was investigated by fluorescence spectroscopy respectively. 4-Nitroaniline can strongly quench intrinsic fluorescence of BSA and HSA. 4-Nitroaniline exhibits a high affinity to bovine and human serum albumins. The binding constantsKand the number binding sitenwere obtained by double-log regression equation. Negative enthalpy (ΔH) and positive entropy (ΔS) values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of 4-nitroaniline and SA. The results of synchronous fluorescence showed the polarity around tryptophan residues was decreased and the hydrophobicity was increased.
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Naz, Farheen, Haider Anis, Ziaul Hasan, Asimul Islam, and Luqman A. Khan. "Exploration of Fungal Lipase as Direct Target of Eugenol through Spectroscopic Techniques." Protein & Peptide Letters 26, no. 12 (October 11, 2019): 919–29. http://dx.doi.org/10.2174/0929866526666190506113455.

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Background:Fungal lipase dependent processes are important for their pathogenicity. Lipases can therefore be explored as direct target of promising herbal antifungals.Objective:We explored Aspergillus niger lipase as a direct target of eugenol through spectroscopic techniques and compare results with Bovine Serum Albumin and lysozyme to comment on selectivity of eugenol towards lipase.Methods:In vitro activity assays of lipase are used to determine concentration ranges. UV-Visible, Fluorescence and Circular dichroism spectroscopy were employed to determine binding constant, stoichiometric binding sites and structural changes in Lipase, BSA and lysozyme following incubation with varying concentrations of eugenol.Results:In activity assays 50% inhibition of lipase was obtained at 0.913 mmoles/litre eugenol. UV-vis spectroscopy shows formation of lipase-eugenol, Bovine Serum Albumin-eugenol and lysozyme-eugenol complex well below this concentration of eugenol. Eugenol binding caused blue shift with Bovine Serum Albumin and lysozyme suggestive of compaction, and red shift with lipase. Negative ellipticity decreased with lipase but increased with Bovine Serum Albumineugenol and lysozyme-eugenol complexes suggesting loss of helical structure for lipase and compaction for Bovine Serum Albumin and lysozyme. Binding of eugenol to lipase was strong (Ka= 4.7 x 106 M-1) as compared to Bovine Serum Albumin and lysozyme. The number of stoichiometric eugenol binding sites on lipase was found to be 2 as compared to 1.37 (Bovine Serum Albumin) and 0.32 (lysozyme). Docking results also suggest strong binding of eugenol with lipase followed by Bovine Serum Albumin and lysozyme.Conclusion:Eugenol is found to be effective inhibitor and disruptor of secondary and tertiary structure of lipase, whereas its binding to Bovine Serum Albumin and lysozyme is found to be weak and less disruptive of structures suggesting selectivity of eugenol towards lipase.
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Shahinyan, Mariam A., Marieta S. Mikaelyan, Marine A. Parsadanyan, and Ara P. Antonyan. "COMPARISON OF METHYL VIOLET INTERACTION WITH BOVINE SERUM ALBUMIN AND HUMAN SERUM ALBUMIN BY UV-DENATURATION METHOD." Proceedings of the YSU B: Chemical and Biological Sciences 56, no. 2 (258) (August 28, 2022): 136–40. http://dx.doi.org/10.46991/pysu:b/2022.56.2.136.

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In the present work the interaction of methyl violet (MV) with human serum albumin (HSA) and bovine serum albumin (BSA) has been studied by the UV-denaturation method and the obtained data were compared. The denaturation parameters – denaturation temperature and denaturation interval width, were determined. It was shown that MV, binding to serum albumins, stabilizes their structure. At the same time, the stabilization degree is different. It was also shown that BSA is stabilized more, than HSA, while binding to MV.
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Chengman Bao, Chengman Bao, Jialian Wang Jialian Wang, Xuehong Tong Xuehong Tong, Chunli Zhang Chunli Zhang, and Xinhui Tang Xinhui Tang. "Interaction of Nitroglycerin with Bovine Serum Albumin and the Influence of Metal Ions on the Binding." Journal of the chemical society of pakistan 42, no. 2 (2020): 180. http://dx.doi.org/10.52568/000626.

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The effect of Cu2+, Ca2+, Mg2+and Zn2+ on the interaction between nitroglycerin and bovine serum albumin was investigated. The bimolecular quenching rate constant, the Stern-Volmer quenching constant, the binding constants and the number of binding sites were calculated in the absence and presence of Cu2+, Ca2+, Mg2+and Zn2+. The quenching constants of nitroglycerin to bovine serum albumin were increased in the presence of metal ions. Static quenching mechanism was also confirmed. The binding constants of nitroglycerin to bovine serum albumin were influenced by different metal ions. The enthalpy change, free energy chang, entropy change and the distance between the donor and the acceptor at different temperatures were calculated. The results indicated that energy transfer from bovine serum albumin to nitroglycerin occurs with high probability.
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Dissertations / Theses on the topic "Bovine serum albumin"

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Marincic, Patricia Z. "Quantitation of Bovine Serum Albumin in Cow's-Milk-Based Infant Formulas and Removal of Bovine Serum Albumin from Cow's Milk and Whey Protein Isolates." DigitalCommons@USU, 1997. https://digitalcommons.usu.edu/etd/5443.

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Early introduction of cow's-milk-based infant formulas, in particular the ABBOS epitope of bovine serum albumin (BSA), has been implicated as an autoimmune trigger in the pathogenesis of insulin dependent diabetes mellitus (IDDM). A direct enzyme-linked immunosorbant assay (ELISA), using polyclonal anti-BSA antibodies, was developed to determine the BSA content of cow's milk and 15 infant formulas. Powdered high-whey (60%) formulas averaged 41 mg BSA/100 ml; 2% milk contained 52 mg BSA/100 ml; and the high-casein formulas averaged 13 mg/100 ml. BSA content of powdered polymeric formulas and cow's milk varied directly with the whey protein concentration (correlation coefficient = 0.8445, Q = 0.008). BSA was not detected in any hydrolyzed powdered formula or commercially sterile liquid preparation regardless of protein composition. The absence of BSA was confirmed by polyacrylamide gel electrophoresis. It is unlikely that the ABBOS epitope is present in the formulas testing negative for BSA due to enzymatic hydrolysis and heat denaturation of these formula preparations. A laboratory technology was developed that could be upgraded to produce BSA free protein bases used in the manufacture of infant formula. Affinity chromatography, using paramagnetic beads with an immobilized antibody against BSA, was applied to extract BSA from cow's milk and whey isolates. Monoclonal and polyclonal antibody-activated beads were used to capture BSA from samples. The capture efficiency in milk was 11% and 19% for polyclonal beads, and 59% for monoclonal beads. Capture efficiency of monoclonal beads of 91% was significantly greater in both acid and sweet whey compared to the polyclonal beads exhibiting a capture efficiency 31% and 24% in acid and sweet whey, respectively. Capture efficiency of monoclonal and polyclonal beads did not differ significantly in milk, acid whey, or sweet whey. Removal of BSA from a known sample of 25ng of BSA treated with polyclonal beads was 70% effective with a capture efficiency of 35%. A net reduction of 99.9% of the BSA could be expected by coupling immunocapture with molecular sieving. Immunocapture was most effective in removing BSA when only small amounts were present in the sample.
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Pfeilsticker, Neves Renata. "Glycated Bovine Serum Albumin for Curcumin Nanoencapsulation: Bio-Nano Interactions." Thesis, Université d'Ottawa / University of Ottawa, 2021. http://hdl.handle.net/10393/42583.

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Glycation of whey proteins results in food-grade composites with modified physicochemical properties. Here, the reaction between glucose and bovine serum albumin (BSA) is promoted under wet-heating conditions. The glycated protein is characterized in depth and compared to the native counterpart and the impact of glycation on properties like net surface charge, particle size and surface hydrophobicity are observed. Conjugation with glucose reduced the surface hydrophobicity of BSA but the interactions between albumin and curcumin became stronger, which contradicts the direct relationship between curcumin binding affinity and protein surface hydrophobicity described in the literature. Nonetheless, curcumin was still capable of quenching the intrinsic fluorescence of the protein after conjugation with glucose and leads to the conclusion that curcumin and BSA interact in a different manner upon glycation. This thesis also depicts mucin as a forthcoming model in the study of nanoparticle interactions with intestinal mucus and glycation posed no effect on such interactions.
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Castro, Ana Carolina Santos de. "Measurement of anti-bovine serum albumin antibodies in dogs with chronic enteropathy." Master's thesis, Universidade de Lisboa, Faculdade de Medicina Veterinária, 2019. http://hdl.handle.net/10400.5/18986.

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Dissertação de Mestrado Integrado em Medicina Veterinária
Chronic Enteropathy (CE) is a complex disease that is thought to result from an overstated immune response against alimentary and microbiota antigens in susceptible animals. The amplified inflammation of the mucosa promoted by the increased and abnormal gut permeability in sick patients known as ‘leaky gut’, allows the antigens to pass through the systemic circulation, culminating in an unbalanced excessive immune response that is followed by the production of specific Immunoglobulins (Ig). Bovine protein is historically believed to be one of the highest immune triggers in dogs with CE. However, studies about the use of anti-bovine serum albumin antibodies (anti-BSAA) as potential biomarkers of a disrupted immune-response in dogs with CE are lacking. This study aimed to compare anti-BSA antibody values (IgA/IgG) between healthy dogs and dogs diagnosed with CE, assessing its potential utility as a biomarker of a leaky gut. A case-control study was conducted including a total of 21 dogs, divided into two distinct groups. The first group consisted on 8 client-owned healthy adult dogs (control group), fed with current adult standard dry diet; the second group was composed by 13 client-owned dogs with clinical signs of CE that historically contacted with standard diets of bovine-protein but were latter fed with an hydrolyzed bovine-free diet for at least two weeks. Serum samples were obtained and anti-BSA Antibodies (IgA/IgG) measured, using a species-specific ELISA kit. There was no significant difference on IgA levels between groups (p= 0,119). Concerning IgG, serial titers were lower in diseased dogs, when compared to the control group (P=0.046). Anti-BSAA do not seem to be good biomarkers of “leaky gut”. A possible explanation for the fact that IgG levels are higher in healthy dogs relies on the diet protein source, which can contain bovine extracts. Assuming that diseased dogs had previously contacted with bovine-proteins, other possibility is that dogs with chronic enteropathy are not able to produce enough immune-globulins, showing a poor humoral immunity towards bovine antigens. Accordingly to previous studies, these results also disbelieves the use of serologic serum profiles to assess potential dietary antigenicity. Albeit bovine protein is historically believed to be one of the highest immune triggers in dogs with CE, these preliminary results supports that anti-BSAA do not seem to be good biomarkers of a “leaky gut”. Further studies are needed to evaluate if low-IgG levels can be related with a poor humoral immune response in dogs with CE.
RESUMO - DETECÇÃO E DOSEAMENTO DE ANTICORPOS SÉRICOS ANTI-ALBUMINA BOVINA EM CÃES COM ENTEROPATIA CRÓNICA - A Enteropatia crónica (EC) é uma doença complexa e multifatorial que se acredita ser resultado de uma resposta imunitária exacerbada a antigénios alimentares e/ou microbianos em animais geneticamente suscetíveis. A inflamação da mucosa intestinal é resultante de uma permeabilidade aumentada da barreira intestinal, o que permite a passagem de antigénios do lúmen para a circulação sistémica. Esta alteração culmina numa resposta imunitária exacerbada com consequente produção inapropriada de imunoglobulinas especificas. A proteína bovina é atualmente aceite como um dos principais desencadeadores imunitários em cães com EC. O presente estudo visa comparar os valores de anticorpos específicos anti-BSA (IgA/IgG) em cães saudáveis e em cães diagnosticados com EC, estimando a potencial utilidade destes como biomarcador de alteração de permeabilidade intestinal (“leaky gut”). Foi efetuado um estudo do tipo caso-controlo que incluiu um total de 21 cães. Estes foram divididos em 2 grupos: grupo controlo (constituído por 8 cães adultos clinicamente saudáveis e alimentados com ração standard para adultos) e um grupo composto por 13 cães com sinais clínicos de EC. Em ambos os grupos foram medidos os anticorpos anti-BSA, através das amostras de soro obtidas e recorrendo a um kit ELISA espécie-específico. Relativamente aos níveis séricos de IgA, não houve diferença significativa entre os dois grupos (p=0,119). No entanto, os níveis de IgG foram significativamente inferiores em cães com EC, quando comparados ao grupo de controlo (p=0,046). O decréscimo observado em cães com EC pode ser explicado por uma eventual produção insuficiente de imunoglobulinas, consequente de uma fraca resposta humoral em relação aos antigénios bovinos. Outra possível explicação para o facto de os níveis de IgG serem mais elevados em cães saudáveis pode residir na origem da proteína animal da dieta, que poderá conter extratos bovinos. Embora se defenda que a proteína bovina seja um dos maiores estímulos imunitários em cães com EC, estes resultados sustentam que os anticorpos anti-BSA não aparentam ser biomarcadores adequados a esta condição. Este trabalho corrobora estudos anteriores que questionam o uso de perfis séricos sorológicos para avaliar a potencial antigenicidade alimentar. São necessários mais estudos para esclarecer se baixos títulos de IgG poderão estar relacionados com uma deficiente resposta imune humoral em cães com CE.
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Yeung, Kai Ming. "The adsorption of bovine serum albumin on fused silica : a single molecules study." HKBU Institutional Repository, 2008. http://repository.hkbu.edu.hk/etd_ra/1017.

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Alansari, Wafa S. "Antioxidant and angiotensin converting enzyme inhibitory activities from bovine serum albumin." Thesis, University of Surrey, 2016. http://epubs.surrey.ac.uk/810091/.

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Bioactive peptides represent an important source of health promoting food. Therefore, the objective of this study was to identify the in vitro antioxidant and ACE inhibitory peptides derived from bovine serum albumin (BSA) and to characterise them after further purification. To achieve this objective, BSA was hydrolyzed with pepsin enzyme, fractionated by ultrafiltration using a 10 kDa molecular weight cut off membrane, and purified by gel filtration chromatography prior to characterisation. The total antioxidant activity was evaluated in a linoleic acid model system using the ferric thiocyanate (FTC) and thiobarbituric acid reactive species (TBARS) methods. The results indicated that gel filtration fraction number 18 exhibited the highest FTC antioxidant activity (65.4 %) compared to the (< 10 kDa) ultrafiltration fraction (44.8 %) and BSA hydrolysate (34.9 %) using a concentration of 1mg peptide/ml. However, the peptide activities were lower than those of 0.01 % butylated hydroxyanisole (69.9 %) and 0.01 % trolox (78.5 %) (P ≤ 0.05). Likewise, TBARS inhibition values were 42.8, 54.8, 76.7 and 84.4 % for BSA hydrolysate, < 10 kDa, BHA and trolox, respectively. The antioxidant activity of the (Mw < 10 kDa) peptide was demonstrated by strong free radical scavenging using the 1, 1-diphenyl-2-picrylhydrazyl (DPPH•), hydroxyl (OH•) and superoxide anion (O2-•); ferric (Fe3+) reducing and ferrous (Fe2+) metal ion chelating capacity and reducing power activity. A second gel filtration fraction number 22 exhibited the highest ACE inhibitory activity (79.5%) compared to the (10 kDa) ultrafiltration fraction (44.7%) and BSA hydrolysate (33.2 %) at a concentration of 10 mg/ml, with corresponding low IC50 values of 0.32, 0.56 and 0.75 mg/ml respectively compared to captopril (88.5%, P ≤ 0.05). The peptide (GF 18) at 1 mg/ml had no cytotoxic effect in epithelial caco-2 cells. Moreover, the presence of the peptide showed high cell viability (99.7%) and reduced malondialdehyde formation (27.7 µg/ml) compared with cells treated with 3mM t-BHP alone, which showed low cell viability (54.6%) and high MDA (30.3 µg/ml) (P < 0.01). BSA peptides protected t-BHP treated cells from caspase-dependent apoptosis; inhibited intracellular ROS production and increased glutathione level and SOD activity. Similarly, the GF 22 peptides (1 mg/ml) protected the endothelial EA.hy 926 against 3mM t-BHP damage and showed reduced mROS production by both lucigenin-enhanced chemiluminescence and the DHE fluorescence techniques. Additionally, the peptides reduced nitrite concentration and inhibited the activity of angiotensin converting enzyme in a dose dependent manner. This study reports novel findings showing that BSA peptides have antioxidant and ACE inhibitory activities that could potentially be used as food supplements and pharmaceutical agents.
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Puckett, Nathan. "Effects of Binding Affinity between Bovine Serum Albumin and Platinum Drugs." TopSCHOLAR®, 2017. http://digitalcommons.wku.edu/theses/1977.

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Platinum complex drugs such as cisplatin have been used as highly successful chemotherapy drugs since the 1970s. We are interested in how the ligands attached to cisplatin analogs influences their reactivity with biologically relevant targets along with time and amount. For this study, reactions were conducted to determine the reactivity between different platinum compounds and the protein bovine serum albumin. Various platinum compounds with different ligands were reacted in varying amounts with albumin in ammonium acetate buffer for either 1 hour, 4 hours, or 24 hours. Each reaction was quenched after the designated reaction time by dialysis and the platinum bound to the protein was determined by use of ICP. LC-MS was used to find exact peptide residues platinum complexes prefer to bind with but was found to be ineffective. Results show that time has a more significant affect on binding over amount of platinum present. In respect to changing the leaving or carrier ligands on the platinum complex, these changes on the complex did not affect binding significantly with bovine serum albumin. Triamine platinum complexes also seem to bind significantly more than diamine platinum complexes along with anionic form platinum complexes binding significantly better than the cationic form platinum complexes.
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Lai, Chun-Chih. "Bovine serum albumin adhesion force measurements using an atomic force microscopy." Thesis, Queensland University of Technology, 2006. https://eprints.qut.edu.au/16418/1/Chun-Chih_Lai_Thesis.pdf.

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In this thesis, a direct method of Atomic Force Microscopy (AFM) technique has been developed to measure the adhesion forces between BSA and two different surfaces: mica (a hydrophilic surface); and polystyrene (a hydrophobic surface); in PBS solution. We have shown possible to measure interactions between proteins and substrate surface directly without any modification to the substrate and the AFM tip; this means protein molecules can keep the natural elastic property within the force measurements. The average measured value of adhesion forces between BSA and mica is 0.036 ± 0.002 nN, and between BSA and polystyrene is 0.066 ± 0.003 nN. The polystyrene surface is more adhesive to BSA than the mica surface. This is consistent with previous research, which assessed that hydrophobic surfaces enhance protein adhesion but hydrophilic surfaces do not.
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Lai, Chun-Chih. "Bovine serum albumin adhesion force measurements using an atomic force microscopy." Queensland University of Technology, 2006. http://eprints.qut.edu.au/16418/.

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In this thesis, a direct method of Atomic Force Microscopy (AFM) technique has been developed to measure the adhesion forces between BSA and two different surfaces: mica (a hydrophilic surface); and polystyrene (a hydrophobic surface); in PBS solution. We have shown possible to measure interactions between proteins and substrate surface directly without any modification to the substrate and the AFM tip; this means protein molecules can keep the natural elastic property within the force measurements. The average measured value of adhesion forces between BSA and mica is 0.036 ± 0.002 nN, and between BSA and polystyrene is 0.066 ± 0.003 nN. The polystyrene surface is more adhesive to BSA than the mica surface. This is consistent with previous research, which assessed that hydrophobic surfaces enhance protein adhesion but hydrophilic surfaces do not.
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Needham, Judy. "Adsorption of bovine serum albumin to polyethylene tubing reversibility and pH-dependence." Thesis, University of British Columbia, 1988. http://hdl.handle.net/2429/28293.

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This thesis is concerned with the adsorption of bovine serum albumin to polyethylene tubing. A method using radioiodinated protein was developed to measure the surface concentration taking into account the dilution effect for miscible displacement in a capillary. A steady-state surface concentration was established within 2 hours. Adsorption did not depend on the ratio of radiolabelled to unlabel led protein. The adsorption isotherm was Langmuir-like with a plateau concentration of approximately 0.2 μg/cm². Two methods were used to calculate the surface concentration in the desorption study. The surface concentration calculated by depletion of the total radioactivity was always higher than that calculated from assaying the radioactivity associated with the tubing. Desorption of at least 5% of the loosely bound protein occurs. The surface concentration-pH data show two maxima. The first is at the isoelectric point of the albumin while the second is at pH 9.5-10. The second maximum seems to be due to preferential adsorption of the higher molecular weight oligomers in the protein sample.
Science, Faculty of
Chemistry, Department of
Graduate
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Franco, Luís Fernando Mercier. "Study on the thermodynamics of bovine serum albumin aqueous solutions: experiments, modeling and molecular simulations." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/3/3137/tde-14072016-140814/.

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The interaction between two proteins into salt aqueous solutions is investigated throughout this thesis. Experiments, modeling and molecular simulations were carried out to get a better understanding of the phenomenon. Bovine serum albumin was used as a model protein. An analytical expression for the structure factor for globular proteins in aqueous solution is presented in this work. This expression was obtained considering an intermolecular potential given by the sum of a hard core, a van der Waals attractive and a screened Coulomb contribution. Experimental data of Small Angle X-Ray Scattering for bovine serum albumin in aqueous solutions containing sodium salts at different protein concentrations and pH values are also presented. The expression developed for the structure factor describes accurately these experimental data provided a dependence of the attractive parameter on protein concentration is established. An expression for the osmotic pressure was derived from the structure factor. With attractive parameters adjusted from X-ray scattering data, the osmotic pressure of bovine serum albumin aqueous solutions could be predicted with very good agreement with experimental data. A derivation of the thermodynamic potentials, such as the chemical potential, using the new osmotic equation of state is presented. Applying the phase equilibrium criterion, the fluid-fluid phase equilibrium for bovine serum albumin in salt aqueous solution was calculated. Although such separation was not experimentally observed at the isoelectric point, it was indeed experimentally observed for a pH value below the isoelectric point. The predictions seem to be valuable to discuss how ion specificity affects the phase diagram of proteins. To apply molecular dynamic techniques to simulate how proteins interact to each other in salt aqueous solutions, two new coarse-grained force fields are proposed. The first one, meant for sodium sulfate aqueous solution, avoids the unphysical association observed for non-polarizable atomistic force fields; and allows the prediction of thermodynamic and dynamic properties. The second one, meant for bovine serum albumin in aqueous solution, is used as a new strategy to evaluate the scattering form factor of proteins as a low resolution technique for protein structure prediction.
Nesta tese apresenta-se uma investigação sobre a interação entre duas proteínas em soluções aquosas salinas. Experimentos, modelagem e simulações moleculares foram realizadas para conseguir um melhor entendimento do fenômeno. Albumina de soro bovina foi usada como proteína modelo. Uma expressão para o fator de estrutura de proteínas globulares em solução aquosa é apresentada neste trabalho. Esta expressão foi obtida considerando-se um potencial intermolecular dado pela soma de um núcleo duro, uma contribuição atrativa tipo vander Waals e uma contribuição de potencial coulômbico blindado. Dados experimentais de espalhamento de raios-X a baixos ângulos para a albumina de soro bovino em soluções aquosas contendo sais de sódio com diferentes concentrações de proteína e valores de pH também são apresentados. A expressão desenvolvida para o fator de estrutura descreve com precisão estes dados experimentais, desde que uma dependência entre o parâmetro atrativo com a concentração de proteína seja estabelecida. Uma expressão para a pressão osmótica foi derivada do fator de estrutura. Com parâmetros atrativos ajustados aos dados de espalhamento de raios-X, a pressão osmótica da albumina de soro bovino em solução aquosa pôde ser predita com grande correlação com os dados experimentais. Uma derivação dos potenciais termodinâmicos usando a nova equação osmótica de estado é apresentada. Aplicando o critério de equilíbrio de fases, foi possível calcular o equilíbrio fluido-fluido para a albumina de soro bovino em solução aquosa. Embora tal separação não tenha sido observada experimentalmente em um pH igual ao ponto isoelétrico, ela foi de fato observada experimentalmente para um valor de pH menor do que o ponto isoelétrico. As predições parecem ser valiosas para discutir como a especificidade iônica afeta o diagrama de fases de proteínas. De modo a avaliar como proteínas interagem umas com as outras usando técnicas de dinâmica molecular, dois novos campos de força coarse-grained são propostos. O primeiro, para o sulfato de sódio em solução aquosa, evita a associação não-física que é observada para campos de força atomísticos não-polarizáveis. Este modelo é capaz de prever propriedades dinâmicas e termodinâmicas. O segundo, para a albumina de soro bovino em solução aquosa, é usado como uma nova estratégia para avaliar o fator de forma de espalhamento de proteínas como uma ferramenta de baixa resolução na predição de estruturas proteicas.
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Books on the topic "Bovine serum albumin"

1

Young, Jeffrey Alan. Evaluation of the interaction of bovine serum albumin and a stearic acid surface film using the Langmuir trough. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1993.

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Masuelli, Martin A. Bovine Serum Albumin: Properties and Applications. Nova Science Publishers, Incorporated, 2020.

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Masuelli, Martin A. Bovine Serum Albumin: Properties and Applications. Nova Science Publishers, Incorporated, 2020.

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Suttiprasit, Prasert. Molecular properties influencing the surface activity of Ü-lactalbumin, Ý-lactoglobulin and bovine serum albumin. 1992.

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Muralidhara, Lakamraju. Resistance of adsorbed nisin to exchange with bovine serum albumin, Ü-lactalbumin, Ý-lactoglobulin, and Ý-casein at silanized silica surfaces. 1994.

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Book chapters on the topic "Bovine serum albumin"

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Reddy, Narendra, and Yiqi Yang. "Regenerated Fibers from Bovine Serum Albumin (BSA)." In Innovative Biofibers from Renewable Resources, 241–44. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-45136-6_53.

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Ernest, Vinita, N. Chandrasekaran, and Amitava Mukherjee. "Colloidal Silver Nanoparticles and Bovine Serum Albumin." In Encyclopedia of Metalloproteins, 701–6. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_526.

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Saito, Masayoshi. "Emulsifying Properties of Bovine Serum Albumin and its Enzymatic Hydrolyzate." In Food Hydrocolloids, 421–27. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2486-1_65.

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Hansen, Paul Robert, Arne Holm, and Gunnar Houen. "Bovine serum albumin: A new support for solid-phase peptide synthesis." In Peptides, 637–38. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_255.

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Sido, Jessica Margaret. "Methylated Bovine Serum Albumin (mBSA)-Induced Delayed-Type Hypersensitivity in Mice." In Methods in Molecular Biology, 95–99. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8549-4_7.

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Shinnar, Ann Eisenberg, Thomas J. Lobl, and Gobi R. Nagarajan. "Precursor peptides of bovine serum albumin exhibit flexibility in backbone conformation." In Peptides, 280–82. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_100.

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Donato, L., C. Garnier, B. Novales, and J. L. Doublier. "Heat-induced gelation of bovine serum albumin- low methoxyl pectin systems." In Special Publications, 227–35. Cambridge: Royal Society of Chemistry, 2009. http://dx.doi.org/10.1039/9781847551214-00227.

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Lai, Chun Chih, John M. Bell, and Nunzio Motta. "Bovine Serum Albumin Adhesion Force Measurements Using an Atomic Force Microscopy." In Frontiers in Materials Science and Technology, 49–52. Stafa: Trans Tech Publications Ltd., 2008. http://dx.doi.org/10.4028/0-87849-475-8.49.

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Mascart-Lemone, F., D. L. Delacroix, S. Cadranel, J. P. Vaerman, and J. Duchateau. "Size Distribution of Serum IgA Antibodies to Food Proteins: Bovine Beta-Lactoglobulin (BLG), Bovine Serum Albumin (BSA) and Gliadin (GL)." In Recent Advances in Mucosal Immunology, 841–46. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5344-7_98.

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Seifert, A., H. M. Rawel, J. Kroll, and S. E. Harding. "Characterization of bovine serum albumin/chlorogenic acid solution mixtures by analytical ultracentrifugation." In Analytical Ultracentrifugation VII, 83–88. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/b98017.

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Conference papers on the topic "Bovine serum albumin"

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Joshi, Narahari V., Virgina O. d. Joshi, Silvia Contreras, Herminia Gil, Honorio Medina, and Aleksander Siemiarczuk. "Fluorescence lifetime measurements of native and glycated human serum albumin and bovine serum albumin." In BiOS '99 International Biomedical Optics Symposium, edited by Joseph R. Lakowicz, Steven A. Soper, and Richard B. Thompson. SPIE, 1999. http://dx.doi.org/10.1117/12.347514.

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Liu, Mingxue, Xiaofeng Pang, Mingxue Liu, Faqin Dong, Wei Zhang, and Jia Tang. "The Interaction between Uranium and Bovine Serum Albumin." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5516517.

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Wang, Feng, Nan Cao, and Wei Huang. "Interaction between carminic acid and bovine serum albumin." In 2016 International Conference on Civil, Transportation and Environment. Paris, France: Atlantis Press, 2016. http://dx.doi.org/10.2991/iccte-16.2016.127.

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Ye, Zhi-Ting, Po-Ju Wu, and Hsin-Ching Kuo. "Feasibility Study of Spectral Detection Bovine Serum Albumin." In 2021 IEEE 6th Optoelectronics Global Conference (OGC). IEEE, 2021. http://dx.doi.org/10.1109/ogc52961.2021.9654321.

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Klos-Witkowska, Aleksandra, Bakhytzhan Akhmetov, Nazym Zhumangalieva, Volodymyr Karpinskyi, and Tomasz Gancarczyk. "Bovine Serum Albumin stability in the context of biosensors." In 2016 16th International Conference on Control, Automation and Systems (ICCAS). IEEE, 2016. http://dx.doi.org/10.1109/iccas.2016.7832427.

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Lazim, Azwan Mat, Regina Sisika A. Sonthanasamy, and Tan Ling Ling. "Binding study of carbon dots to bovine serum albumin." In THE 2018 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2018 Postgraduate Colloquium. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5111260.

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Cherkasova, Olga P., Maxim M. Nazarov, and Alexander P. Shkurinov. "Investigation of bovine serum albumin glycation by THz spectroscopy." In Saratov Fall Meeting 2015, edited by Elina A. Genina, Valery V. Tuchin, Vladimir L. Derbov, Dmitry E. Postnov, Igor V. Meglinski, Kirill V. Larin, and Alexander B. Pravdin. SPIE, 2016. http://dx.doi.org/10.1117/12.2229741.

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Tay, Li-Lin, Nelson L. Rowell, David J. Lockwood, and Rabah Boukherroub. "Bovine serum albumin adsorption on functionalized porous silicon surfaces." In Photonics North, edited by John C. Armitage, Roger A. Lessard, and George A. Lampropoulos. SPIE, 2004. http://dx.doi.org/10.1117/12.567386.

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Feng, Shangyuan, Juqiang Lin, Yongzeng Li, Zufang Huang, and Rong Chen. "Binding Interactions of Hematoporphyrin Monomethyl Ether with Bovine Serum Albumin." In 2008 IEEE PhotonicsGlobal@Singapore (IPGC). IEEE, 2008. http://dx.doi.org/10.1109/ipgc.2008.4781390.

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Shaban, Hassanein, Mon-Juan Lee, and Wei Lee. "Optical Detection of Bovine Serum Albumin by Lyotropic Liquid Crystal." In Frontiers in Optics. Washington, D.C.: OSA, 2020. http://dx.doi.org/10.1364/fio.2020.fth1d.6.

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Reports on the topic "Bovine serum albumin"

1

Spiegel, Yitzhak, Michael McClure, Itzhak Kahane, and B. M. Zuckerman. Characterization of the Phytophagous Nematode Surface Coat to Provide New Strategies for Biocontrol. United States Department of Agriculture, November 1995. http://dx.doi.org/10.32747/1995.7613015.bard.

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Chemical composition and biological role of the surface coat (SC) of the root-knot nematodes, Meloidogyne spp. are described. SC proteins of M. incognita race 3 infective juveniles (J2) were characterized by electrophoresis and western blotting of extracts from radioiodine and biotin-labelled nematodes. J2 labelled with radioiodine and biotin released 125I and biotin-labelled molecules into water after 20 hours incubation, indicating that SC proteins may be loosely attached to the nematode. Antiserum to the principal protein reacted with the surface of live J2 and with surface proteins previously separated by electrophoresis. Human red blood cells (HRBC) adhered to J2 of several tylenchid nematodes over the entire nematode body. HRBC adhered also to nylon fibers coated with SC extracted from M. javanica J2; binding was Ca++/Mg++ dependent, and decreased when the nylon fibers were coated with bovine serum albumin, or pre-incubated with fucose and mannose. These experiments support a working hypothesis that RBC adhesion involves carbohydrate moieties of HRBC and carbohydrate-recognition domain(s) (CRD) distributed on the nematode surface. To our knowledge, this is the first report of a surface CRD i the phylum Nematoda. Gold-conjugated lectins and neoglycoproteins combined with silver enhancement have been used for the detection of carbohydrates and CRD, respectively, on the SC of M. javanica J2. Biotin reagents were used to trace surface proteins, specifically, on live J2. The labile and transitory nature of the SC was demonstrated by the dynamics of HRBC adherence to detergent-treated J2, J2 at different ages or fresh-hatched J2 held at various temperatures. SC recovery was demonstrated also by a SDS-PAGE profile. Monoclonal antibodies developed to a cuticular protein of M. incognita J2 gave a slight, but significant reduction in attachment of Pasteuria penetrans spores. Spore attachment as affected by several enzymes was inconsistent: alcian blue, which specifically blocks sulfyl groups, had no afffect on spore attachment. Treatment with cationized ferritin alone or catonized ferritin following monoclonal antibody caused significant decreases in spore attachment. Those results suggest a role in attachment by negatively charged groups.
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Sela, Shlomo, and Michael McClelland. Investigation of a new mechanism of desiccation-stress tolerance in Salmonella. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7598155.bard.

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Low-moisture foods (LMF) are increasingly involved in foodborne illness. While bacteria cannot grow in LMF due to the low water content, pathogens such as Salmonella can still survive in dry foods and pose health risks to consumer. We recently found that Salmonella secretes a proteinaceous compound during desiccation, which we identified as OsmY, an osmotic stress response protein of 177 amino acids. To elucidate the role of OsmY in conferring tolerance against desiccation and other stresses in Salmonella entericaserovarTyphimurium (STm), our specific objectives were: (1) Characterize the involvement of OsmY in desiccation tolerance; (2) Perform structure-function analysis of OsmY; (3) Study OsmY expression under various growth- and environmental conditions of relevance to agriculture; (4) Examine the involvement of OsmY in response to other stresses of relevance to agriculture; and (5) Elucidate regulatory pathways involved in controlling osmY expression. We demonstrated that an osmY-mutant strain is impaired in both desiccation tolerance (DT) and in long-term persistence during cold storage (LTP). Genetic complementation and addition of a recombinantOsmY (rOsmY) restored the mutant survival back to that of the wild type (wt). To analyze the function of specific domains we have generated a recombinantOsmY (rOsmY) protein. A dose-response DT study showed that rOsmY has the highest protection at a concentration of 0.5 nM. This effect was protein- specific as a comparable amount of bovine serum albumin, an unrelated protein, had a three-time lower protection level. Further characterization of OsmY revealed that the protein has a surfactant activity and is involved in swarming motility. OsmY was shown to facilitate biofilm formation during dehydration but not during bacterial growth under optimal growth conditions. This finding suggests that expression and secretion of OsmY under stress conditions was potentially associated with facilitating biofilm production. OsmY contains two conserved BON domains. To better understand the role of the BON sites in OsmY-mediated dehydration tolerance, we have generated two additional rOsmY constructs, lacking either BON1 or BON2 sites. BON1-minus (but not BON2) protein has decreased dehydration tolerance compared to intact rOsmY, suggesting that BON1 is required for maximal OsmY-mediated activity. Addition of BON1-peptide at concentration below 0.4 µM did not affect STm survival. Interestingly, a toxic effect of BON1 peptide was observed in concentration as low as 0.4 µM. Higher concentrations resulted in complete abrogation of the rOsmY effect, supporting the notion that BON-mediated interaction is essential for rOsmY activity. We performed extensive analysis of RNA expression of STm undergoing desiccation after exponential and stationary growth, identifying all categories of genes that are differentially expressed during this process. We also performed massively in-parallel screening of all genes in which mutation caused changes in fitness during drying, identifying over 400 such genes, which are now undergoing confirmation. As expected OsmY is one of these genes. In conclusion, this is the first study to identify that OsmY protein secreted during dehydration contributes to desiccation tolerance in Salmonella by facilitating dehydration- mediated biofilm formation. Expression of OsmY also enhances swarming motility, apparently through its surfactant activity. The BON1 domain is required for full OsmY activity, demonstrating a potential intervention to reduce pathogen survival in food processing. Expression and fitness screens have begun to elucidate the processes of desiccation, with the potential to uncover additional specific targets for efforts to mitigate pathogen survival in desiccation.
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3

Landau, Sergei Yan, John W. Walker, Avi Perevolotsky, Eugene D. Ungar, Butch Taylor, and Daniel Waldron. Goats for maximal efficacy of brush control. United States Department of Agriculture, March 2008. http://dx.doi.org/10.32747/2008.7587731.bard.

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Background. Brush encroachment constitutes a serious problem in both Texas and Israel. We addressed the issue of efficacy of livestock herbivory - in the form of goat browsing - to change the ecological balance to the detriment of the shrub vegetation. Shrub consumption by goats is kept low by plant chemical defenses such as tannins and terpenes. Scientists at TAES and ARO have developed an innovative, cost-effective methodology using fecal Near Infrared Spectrometry to elucidate the dietary percentage of targeted, browse species (terpene-richredberry and blueberry juniper in the US, and tannin-rich Pistacialentiscus in Israel) for a large number of animals. The original research objectives of this project were: 1. to clarify the relative preference of goat breeds and the individual variation of goats within breeds, when consuming targeted brush species; 2. to assess the heritability of browse intake and validate the concept of breeding goat lines that exhibit high preference for chemically defended brush, using juniper as a model; 3. to clarify the relative contributions of genetics and learning on the preference for target species; 4. to identify mechanisms that are associated with greater intake of brush from the two target species; 5. to establish when the target species are the most vulnerable to grazing. (Issue no.5 was addressed only partly.) Major conclusions, solutions, achievements: Both the Israel and US scientists put significant efforts into improving and validating the technique of Fecal NIRS for predicting the botanical composition of goat diets. Israeli scientists validated the use of observational data for calibrating fecal NIRS, while US scientists established that calibrations could be used across animals differing in breed and age but that caution should be used in making comparisons between different sexes. These findings are important because the ability to select goat breeds or individuals within a breed for maximal efficiency of brush control is dependent upon accurate measurement of the botanical composition of the diet. In Israel it was found that Damascus goats consume diets more than twice richer in P. lentiscus than Mamber or Boer goats. In the US no differences were found between Angora and Boer cross goats but significant differences were found between individuals within breeds in juniper dietary percentage. In both countries, intervention strategies were found that further increased the consumption of the chemically defended plant. In Israel feeding polyethylene glycol (PEG, MW 4,000) that forms high-affinity complexes with tannins increased P. lentiscus dietary percentage an average of 7 percentage units. In the US feeding a protein supplement, which enhances rates of P450-catalyzed oxidations and therefore the rate of oxidation of monoterpenes, increased juniper consumption 5 percentage units. However, the effects of these interventions were not as large as breed or individual animal effects. Also, in a wide array of competitive tannin-binding assays in Israel with trypsin, salivary proteins did not bind more tannic acid or quebracho tannin than non-specific bovine serum albumin, parotid saliva did not bind more tannins than mixed saliva, no response of tannin-binding was found to levels of dietary tannins, and the breed effect was of minor importance, if any. These fundings strongly suggest that salivary proteins are not the first line of defense from tannin astringency in goats. In the US relatively low values for heritability and repeatability for juniper consumption were found (13% and 30%, respectively), possibly resulting from sampling error or non-genetic transfer of foraging behavior, i.e., social learning. Both alternatives seem to be true as significant variation between sequential observations were noted on the same animal and cross fostering studies conducted in Israel demonstrated that kids raised by Mamber goats showed lower propensity to consume P. lentiscus than counterparts raised by Damascus goats.
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