Journal articles: '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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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/jcsp/42.02.2020.

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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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Topală, Tamara, Andreea Bodoki, Luminiţa Oprean, and Radu Oprean. "Bovine serum albumin interactions with metal complexes." Medicine and Pharmacy Reports 87, no. 4 (November 12, 2014): 215–19. http://dx.doi.org/10.15386/cjmed-357.

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The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum albumins play a key role in drug pharmacokinetics and pharmacodynamics, the study of coordination compounds affinity towards this class of proteins, as well as understanding the mechanism through which they interact is crucial. The aim of this review is to focus on the structure and biological functions of bovine serum albumin, the design of metal complexes that are able to bind to the biomolecule, as well as the experimental techniques employed in the study and evaluation of these interactions. Keywords: drug-protein interaction, coordination complex, fluorescence spectroscopy, UV-Vis absorption spectroscopy.

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Batt, PA, and BG Miller. "Development of Sheep Embryos in vitro in a Medium Supplemented with Different Batches of Serum Albumin." Australian Journal of Biological Sciences 41, no. 3 (1988): 371. http://dx.doi.org/10.1071/bi9880371.

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Variability in different lots of commercial serum albumin affects mammalian embryo development in culture. The composition of commercial preparations of ovine, bovine and defatted bovine serum albumin and a fraction of ovine serum containing proteins with a mean molecular weight of 65 kDa (fraction 3) was examined by polyacrylamide gel electrophoresis. All preparations were heavily contaminated with serum proteins other than albumin. Day-6 sheep morulae were cultured for 48 h in a basal bicarbonate-buffered salt solution supplemented with the commercial preparations of ovine, bovine or defatted bovine serum albumin. These three albumin preparations differed in their abilities to support the development of morulae into expanded blastocysts, but these differences disappeared when the basal medium was also supplemented with a component of ovine serum containing substances with molecular weights of less than 10 kDa. In the latter case, the three commercial albumin preparations and fraction 3 of ovine serum all supported full development in about 40-60% of morulae.

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Andersson, Lars-Olov. "HETEROGENEITY OE DEFATTED BOVINE SERUM ALBUMIN." International Journal of Protein Research 1, no. 1-4 (January 9, 2009): 151–55. http://dx.doi.org/10.1111/j.1399-3011.1969.tb01637.x.

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Kanny, Gisèle, Cécile de Hauteclocque, and Denise-Anne Moneret-Vautrin. "Food anaphylaxis to bovine serum albumin." Journal of Allergy and Clinical Immunology 101, no. 1 (January 1998): 137–39. http://dx.doi.org/10.1016/s0091-6749(98)70210-6.

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Jayabharathi, J., V. Thanikachalam, and K. Jayamoorthy. "Antioxidant benzimidazole bind bovine serum albumin." Journal of Photochemistry and Photobiology B: Biology 115 (October 2012): 85–92. http://dx.doi.org/10.1016/j.jphotobiol.2012.06.014.

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Sano, Yoh. "Optical anisotropy of bovine serum albumin." Journal of Colloid and Interface Science 124, no. 2 (August 1988): 403–6. http://dx.doi.org/10.1016/0021-9797(88)90178-6.

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Bauer, Michael, Joachim Baumann, and Wolfgang E. Trommer. "ATP binding to bovine serum albumin." FEBS Letters 313, no. 3 (November 30, 1992): 288–90. http://dx.doi.org/10.1016/0014-5793(92)81211-4.

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Beretta, Barbara, Amedeo Conti, Alessandro Fiocchi, Antonella Gaiaschi, Corrado L. Galli, Maria Gabriella Giuffrida, Cinzia Ballabio, and Patrizia Restani. "Antigenic Determinants of Bovine Serum Albumin." International Archives of Allergy and Immunology 126, no. 3 (2001): 188–95. http://dx.doi.org/10.1159/000049513.

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Zhou, J. L., Su Yun Yang, C. S. Zhai, Z. M. Cheng, Shu Qian Wu, and G. Q. Wu. "Tribological Characteristics of Silicon Nitride Ceramic in Three Water-Based Lubricants." Key Engineering Materials 642 (April 2015): 99–103. http://dx.doi.org/10.4028/www.scientific.net/kem.642.99.

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The friction coefficient of tribology pair between silicon nitride ceramic and stainless steel was researched with bovine serum albumin, saline and water lubricants. The coefficient of friction of silicon nitride in bovine serum albumin is lower than those in saline and water. Using digital microscope, the worn surfaces of silicon nitride and stainless steel were viewed. The groove depths of worn stainless steel surface were measured. The depth with bovine serum albumin is shallower than those in saline and water. The results showed that ceramic in bovine serum albumin has good tribological characteristic. This research provides the reference for the development of ceramic artificial joint.

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Golianová, Katarína, Samuel Havadej, Valéria Verebová, Jozef Uličný, Beáta Holečková, and Jana Staničová. "Interaction of Conazole Pesticides Epoxiconazole and Prothioconazole with Human and Bovine Serum Albumin Studied Using Spectroscopic Methods and Molecular Modeling." International Journal of Molecular Sciences 22, no. 4 (February 15, 2021): 1925. http://dx.doi.org/10.3390/ijms22041925.

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The interactions of epoxiconazole and prothioconazole with human serum albumin and bovine serum albumin were investigated using spectroscopic methods complemented with molecular modeling. Spectroscopic techniques showed the formation of pesticide/serum albumin complexes with the static type as the dominant mechanism. The association constants ranged from 3.80 × 104–6.45 × 105 L/mol depending on the pesticide molecule (epoxiconazole, prothioconazole) and albumin type (human or bovine serum albumin). The calculated thermodynamic parameters revealed that the binding of pesticides into serum albumin macromolecules mainly depended on hydrogen bonds and van der Waals interactions. Synchronous fluorescence spectroscopy and the competitive experiments method showed that pesticides bind to subdomain IIA, near tryptophan; in the case of bovine serum albumin also on the macromolecule surface. Concerning prothioconazole, we observed the existence of an additional binding site at the junction of domains I and III of serum albumin macromolecules. These observations were corroborated well by molecular modeling predictions. The conformation changes in secondary structure were characterized by circular dichroism, three-dimensional fluorescence, and UV/VIS absorption methods.

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Karapetyan, Nelli H., Lusine R. Aloyan, Robert K. Ghazaryan, and Yevgeni Mamasakhlisov. "Complexes of bovine serum albumin with water-soluble Cu and Co containing cationic meso-tetra(4-N-oxyethylpyridyl)-porphyrins." Journal of Porphyrins and Phthalocyanines 11, no. 07 (July 2007): 475–80. http://dx.doi.org/10.1142/s1088424607000540.

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Bovine serum albumin complexes with water-soluble cationic porphyrins, Cu - and Co-meso-tetra(4- N -hydroxyethylpyridyl)porphyrins ( CuT4OEPyP , CoT4OEPyP ), and their 3- N -analogs, meso-tetra(3- N -hydroxyethylpyridyl)porphyrins ( CuT3OEPyP , CoT3OEPyP ), have been investigated. The porphyrin-bovine serum albumin binding was monitored by the absorption in the visible region at 400-460 nm. The stoichiometry of binding and the binding constants of the porphyrins to bovine serum albumin were determined using binding isotherms and Scatchard plots. The K b values obtained for these porphyrin- bovine serum albumin complexes are 1.7 × 105 M −1, 3.2 × 105 M −1, 1.4 × 105 M −1 and 3 × 105 M −1 respectively. Binding constants are sensitive to pH and ionic strength of the solution.

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Gu, Xiaomin, Fei Ji, Dawei Jiang, Wenhui Liang, Yan Feng, Shanshan Niu, and Qiang Zhao. "The development and application of glyco-probes for bovine serum albumin." Journal of Chemical Research 47, no. 3 (May 2023): 174751982311779. http://dx.doi.org/10.1177/17475198231177954.

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Two glyco-probes, GFP and GFN, which are derived from the condensation of 3-acetyl-5-C-(2,3-dihydroxy-1,4-anhydro-β-D-erythro-tetrofuranosyl)-2-methylfuran with benzaldehyde and 1-naphthaldehyde, respectively, are designed and synthesized. Of these two probes, GFP displays a selective and sensitive switch-on fluorescence response towards bovine serum albumin in phosphate-buffered saline over a wide pH range. Moreover, the fluorescence of this probe displays a good linear relationship with the bovine serum albumin concentration ranging from 0 to 0.8 mg/mL, and has a limit of detection as low as 3.7 nM. The stoichiometric ratio of bovine serum albumin /GFP is 1:1. This research paves the way for the development of glyco-probes for bovine serum albumin sensing.

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Lang, John D., Mario Figueroa, Phillip Chumley, Mutay Aslan, John Hurt, Margaret M. Tarpey, Beatriz Alvarez, Rafael Radi, and Bruce A. Freeman. "Albumin and Hydroxyethyl Starch Modulate Oxidative Inflammatory Injury to Vascular Endothelium." Anesthesiology 100, no. 1 (January 1, 2004): 51–58. http://dx.doi.org/10.1097/00000542-200401000-00012.

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Background Human serum albumin is used clinically to maintain colloid osmotic pressure and is viewed to serve an antioxidant role in the vascular compartment via binding of redox-active metal complexes, transport of nitric oxide, and the oxidant-scavenging reactions of the single thiol of human serum albumin, cys34. Because of these potentially desirable adjunctive actions, we evaluated the purity and thiol redox state and compared the relative effects of clinically available 25% human serum albumin preparations with a starch-derived colloid, 6% hydroxyethyl starch, in in vitro models of inflammatory vascular injury. Methods Bovine aortic endothelial cell responses to chemical, enzymatic, and cell-derived reactive inflammatory mediators in the presence of human serum albumin or hydroxyethyl starch were assessed. Results The cys34 thiol of fresh human serum albumin preparations was 70-85% oxidized and contained a population of human serum albumin (approximately 25% of total) having the cys34 resistant to reduction by 2-mercaptoethanol and NaBH4. Treatment of bovine aortic endothelial cells with human serum albumin dose-dependently protected from HOCl-mediated 14C-adenine release, with this protective effect of human serum albumin not dependent on protein thiol status. Addition of human serum albumin to cell media provided no protection from the cytotoxic actions of peroxynitrite and xanthine oxidase-derived reactive species. Binding of activated polymorphonuclear leukocytes to bovine aortic endothelial cells was significantly amplified by hydroxyethyl starch and inhibited by human serum albumin administration. The binding of neutrophil-derived myeloperoxidase to bovine aortic endothelial cells, a mediator of multiple oxidative and nitric oxide-consuming reactions, was also inhibited by human serum albumin and enhanced by hydroxyethyl starch. Conclusions Clinical human serum albumin preparations show modest intrinsic non-thiol-dependent antiinflammatory properties in vitro, a phenomenon that was not observed with hydroxyethyl starch.

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Kapatsa, G., G. E. Spates, C. L. Sheffield, and J. R. DeLoach. "Comparison of lipid-free haemoglobin and stroma-contaminated haemoglobin diets for adults of Stomoxys calcitrans (L.) (Diptera: Muscidae)." Bulletin of Entomological Research 79, no. 1 (March 1989): 41–45. http://dx.doi.org/10.1017/s0007485300018551.

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AbstractAdults of Stomoxys calcitrans (L.) that fed on stroma-contaminated haemoglobin plus bovine serum albumin had normal survival, fecundity and egg hatch. Feeding on haemoglobin from which the erythrocyte membrane strome had been removed, together with bovine serum albumin, reduced fecundity to zero. The addition of membrane ghost preparation to a lipid-free haemoglobin and bovine serum albumin diet restored the essential nutrients for normal fly fecundity. For normal reproduction therefore, S. calcitrans adults require erythrocyte stroma.

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Kumar, RaviShankar, and Anjali Jha Anjali Jha. "Synthesis of Silver Nanoparticles Using Bovine Serum Albumin, Characterization and Their Bioevaluation." Indian Journal of Applied Research 3, no. 10 (October 1, 2011): 1–3. http://dx.doi.org/10.15373/2249555x/oct2013/129.

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Malarkani, Karpagaraj, Ivy Sarkar, and Susithra Selvam. "Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity." Journal of Pharmaceutical Analysis 8, no. 1 (February 2018): 27–36. http://dx.doi.org/10.1016/j.jpha.2017.06.007.

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Mavropoulos, Elena, Nilce C. C. da Rocha, Maria Helena M. Rocha-Leão, and Antonella M. Rossi. "BSA Adsorption on Hydroxyapatite after Thermal Treatment." Key Engineering Materials 361-363 (November 2007): 127–30. http://dx.doi.org/10.4028/www.scientific.net/kem.361-363.127.

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Adsorption experiments of bovine serum albumin on hydroxyapatite previously annealed at temperatures up to 1100°C was performed at 37°C and phosphate buffer, pH 6.0. Kinetic process was very efficient and irreversible for low phosphate buffer concentration. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HA specific surface area and the number of surface active sites. However, it was verified that particle size was also an important parameter for bovine serum albumin immobilization.

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Jones, K. L., and M. E. Westhusin. "Effect of polyvinyl alcohol, bovine serum albumin fraction V, fetal calf serum and fetal calf serum plus bovine serum albumin fraction V on bovine embryo development." Theriogenology 45, no. 1 (January 1996): 205. http://dx.doi.org/10.1016/0093-691x(96)84678-4.

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Mucha, Martin, Roman Maršálek, Marta Bukáčková, and Gabriela Zelenková. "Interaction among clays and bovine serum albumin." RSC Advances 10, no. 72 (2020): 43927–39. http://dx.doi.org/10.1039/d0ra01430c.

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Song, Yuanzhi, Jimin Xie, Yunlong Wu, Min Chen, Ganqing Zhao, Xiaomeng Lv, Huoming Shu, and Songtao Chen. "Interaction between Phenols and Bovine Serum Albumin." Anti-Infective Agents in Medicinal Chemistry 8, no. 3 (July 1, 2009): 268–71. http://dx.doi.org/10.2174/187152109788680234.

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She-Ying, DONG, XUE Chun-Xia, and HUANG Ting-Lin. "Interaction between Atorvastatin Calciumand Bovine Serum Albumin." Acta Physico-Chimica Sinica 23, no. 10 (2007): 1520–24. http://dx.doi.org/10.3866/pku.whxb20071007.

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Madeira, Pedro P., Inês L. D. Rocha, Marguerita E. Rosa, Mara G. Freire, and João A. P. Coutinho. "On the aggregation of bovine serum albumin." Journal of Molecular Liquids 349 (March 2022): 118183. http://dx.doi.org/10.1016/j.molliq.2021.118183.

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34

Maruthamuthu, Meenakshi, and Sankaran Kishore. "Binding of ketoprofen with bovine serum albumin." Proceedings / Indian Academy of Sciences 99, no. 3 (September 1987): 187–93. http://dx.doi.org/10.1007/bf02880901.

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35

Gülsu, Aydan, Mutlu Can Aslanpay, Mehlika Alper, and Hatice Güneş. "Doxorubicin Release from Bovine Serum Albumin Microparticles." Pharmaceutical Chemistry Journal 55, no. 11 (February 2022): 1157–62. http://dx.doi.org/10.1007/s11094-022-02552-y.

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Seredych, Mykola, Kathleen Maleski, Tyler S. Mathis, and Yury Gogotsi. "Delamination of MXenes using bovine serum albumin." Colloids and Surfaces A: Physicochemical and Engineering Aspects 641 (May 2022): 128580. http://dx.doi.org/10.1016/j.colsurfa.2022.128580.

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AOKI, Koichiro, Hideyuki ANDO, and Koichi HIRAMATSU. "Interaction between Bovine Serum Albumin and Bilirubin." Journal of Japan Oil Chemists' Society 40, no. 9 (1991): 725–29. http://dx.doi.org/10.5650/jos1956.40.725.

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38

Bercea, Maria, Simona Morariu, Ioana-Alexandra Plugariu, and Doina Bărâlă. "Shear flow of bovine serum albumin solutions." Studia Universitatis Babeș-Bolyai Chemia 64, no. 3 (September 30, 2019): 121–28. http://dx.doi.org/10.24193/subbchem.2019.3.10.

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HIROSE, MASAAKI, YURIKO NISHIZAWA, and JIN YOUNG LEE. "Gelation of Bovine Serum Albumin by Glutathione." Journal of Food Science 55, no. 4 (July 1990): 915–17. http://dx.doi.org/10.1111/j.1365-2621.1990.tb01564.x.

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Quiming, Noel Samson, Rex Bugante Vergel, Marilou Gagalac Nicolas, and James Amador Villanueva. "Interaction of Bovine Serum Albumin and Metallothionein." JOURNAL OF HEALTH SCIENCE 51, no. 1 (2005): 8–15. http://dx.doi.org/10.1248/jhs.51.8.

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Choi, P. ‐K, J. ‐R Bae, and K. Takagi. "Ultrasonic spectroscopy in bovine serum albumin solutions." Journal of the Acoustical Society of America 87, no. 2 (February 1990): 874–81. http://dx.doi.org/10.1121/1.398897.

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42

Bojesen, Inge N., and Harald S. Hansen. "Binding of anandamide to bovine serum albumin." Journal of Lipid Research 44, no. 9 (July 1, 2003): 1790–94. http://dx.doi.org/10.1194/jlr.m300170-jlr200.

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43

Choi, Pak‐Kon, Jung‐Rim Bae, and Kenshiro Takagi. "Ultrasonic spectroscopy in bovine serum albumin solutions." Journal of the Acoustical Society of America 84, S1 (November 1988): S139. http://dx.doi.org/10.1121/1.2025804.

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KESSLER, KURT F., ROLF F. BARTH, and KIN-PING WONG. "Physicochemical studies of dinitrophenylated bovine serum albumin." International Journal of Peptide and Protein Research 20, no. 1 (January 12, 2009): 73–80. http://dx.doi.org/10.1111/j.1399-3011.1982.tb02655.x.

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45

MURTHY, N. V. KISHORE KUMAR, and M. S. NARASINGA RAO. "Interaction of allylisothiocyanate with bovine serum albumin." International Journal of Peptide and Protein Research 27, no. 4 (January 12, 2009): 433–39. http://dx.doi.org/10.1111/j.1399-3011.1986.tb01038.x.

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46

Thamwattana, Ngamta, Duangkamon Baowan, and Barry J. Cox. "Modelling bovine serum albumin inside carbon nanotubes." RSC Advances 3, no. 45 (2013): 23482. http://dx.doi.org/10.1039/c3ra43991g.

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47

Mandeville, J. S., and H. A. Tajmir-Riahi. "Complexes of Dendrimers with Bovine Serum Albumin." Biomacromolecules 11, no. 2 (February 8, 2010): 465–72. http://dx.doi.org/10.1021/bm9011979.

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48

Dixit, Rakesh, Mukul Das, Prahlad K. Seth, and Hasan Mukhtar. "Interaction of acrylamide with bovine serum albumin." Environmental Research 40, no. 2 (August 1986): 365–71. http://dx.doi.org/10.1016/s0013-9351(86)80111-6.

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Flores, Juana Rodriguez, Richard O'Kennedy, and Malcolm R. Smyth. "Adsorptive stripping voltammetry of bovine serum albumin." Analytica Chimica Acta 212 (1988): 355–58. http://dx.doi.org/10.1016/s0003-2670(00)84163-x.

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50

Veerman, Cecile, Leonard M. C. Sagis, Jeroen Heck, and Erik van der Linden. "Mesostructure of fibrillar bovine serum albumin gels." International Journal of Biological Macromolecules 31, no. 4-5 (January 2003): 139–46. http://dx.doi.org/10.1016/s0141-8130(02)00074-0.

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Journal articles on the topic 'Bovine serum albumin'

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