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1

Tan, G. X., Ying De Cui, and Ying Jun Wang. "Studies on Characteristics and Adsorption of BSA on Hydrogel Biomaterials." Key Engineering Materials 330-332 (February 2007): 901–4. http://dx.doi.org/10.4028/www.scientific.net/kem.330-332.901.

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Hydrogel biomaterials were synthesized by radical copolymerization of N-vinyl pyrrolidone (NVP) and 2-hydroxyethylmathacrylate (HEMA), with azobisisobutyronitrile (AIBN) as an initiator, reacting at 60~70°C for 24 hours, which were designed as contact lens due to the good chemical stability and high biocompatibility. The absorbency of bovine serum albumin (BSA) was measured by the ultraviolet spectrophotometer. The influence of pH, initial protein concentration and ionic strength were investigated in detail. The results showed that the absorption of protein on hydrogel biomaterials increased w
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2

He, Ling Ling, Xin Wang, Bin Liu, and Rui Mei Xu. "Electrochemical Behavior of Promethazine Hydrochloride and its Interaction with Bovine Serum Albumin." Advanced Materials Research 554-556 (July 2012): 450–53. http://dx.doi.org/10.4028/www.scientific.net/amr.554-556.450.

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In this paper, the electrochemical behavior of promethazine hydrochloride (PMT) and its interaction with bovine serum albumin (BSA) were studied by means of cyclic voltammetry. In pH 6.5 Tris-HCl buffer solution, PMT exhibits a pair of reversible peaks and an irreversible oxidation peak at a bare gold electrode. The electrode reactions are the process controlled by adsorption. The results of cyclic voltammetry suggest that a BSA-PMT complex is formed, and this complex is not electroactive. The absorption spectra confirm the binding PMT to BSA. The binding number m and the binding constant β of
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3

Sorrells, Matthew G., and Keith B. Neeves. "Adsorption and Absorption of Collagen Peptides to Polydimethlysiloxane and Its Influence on Platelet Adhesion Flow Assays." Micromachines 11, no. 1 (2020): 62. http://dx.doi.org/10.3390/mi11010062.

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Collagen peptides are an alternative to animal derived collagens for platelet function studies under flow. The purpose of this study was to examine the use of collagen peptides in polydimethylsiloxane (PDMS) devices. Three collagen peptides with amino acid sequences and structures that capture von Willebrand factor and bind it with the platelet receptors integrin α2β1 and glycoprotein VI were patterned on glass, silicon, and PDMS. Each of these surfaces was also functionalized with tridecafluoro-1,1,2,2-tetrahydrooctyltrichlorosilane (FOTS). Surfaces were characterized by their ability to supp
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4

Wu, N., Jie Weng, Shu Xin Qu, Jian Xin Wang, Xiong Lu, and Bo Feng. "Hydroxyapatite Formation and Protein Absorption on Triethyl Phosphate Modified Titanium Surface." Advanced Materials Research 26-28 (October 2007): 797–800. http://dx.doi.org/10.4028/www.scientific.net/amr.26-28.797.

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In this work, triethyl phosphate (TEP) was used to bioactivating titanium. Titanium plates grafted with TEP were immersed in a two times concentrated simulated body fluid (2SBF) to investigate deposition of hydoxyapatite (HA) on the surface. A phosphate buffer solution (PBS) with bovine serum albumin (BSA) was used to evaluate adsorption of protein on the grafted titanium surface. The morphology, component and structure of samples were examined by scanning electronic microscopy, attenuated total reflection Fourier transform infrared spectroscopy and X-ray diffraction respectively. The concentr
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5

Premetis, Georgios E., and Nikolaos E. Labrou. "Reduce, Reuse and Recycle in Protein Chromatography: Development of an Affinity Adsorbent from Waste Paper and Its Application for the Purification of Proteases from Fish By-Products." Biomolecules 10, no. 6 (2020): 822. http://dx.doi.org/10.3390/biom10060822.

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In the present study, we report the development of a cellulose-based affinity adsorbent and its application for the purification of proteases from fish by-products. The affinity adsorbent was synthesized using cellulose microfibers as the matrix, isolated from recycled newspapers using the acid precipitation method. As an affinity ligand, the triazine dye Cibacron Blue 3GA (CB3GA) was used and immobilized directly onto the cellulose microfibers. Absorption equilibrium studies and frontal affinity chromatography were employed to evaluate the chromatographic performance of the adsorbent using as
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6

Hongkachern, Tippavan, Verawat Champreda, Toemsak Srikhirin, Thidarat Wangkam, and Tanakorn Osotchan. "Effect of pH on the Formation of a Bovine Serum Albumin Layer on a Poly(stryren-co-maleic Acid) Surface." Advanced Materials Research 93-94 (January 2010): 583–86. http://dx.doi.org/10.4028/www.scientific.net/amr.93-94.583.

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The layer formation of bovine serum albumin (BSA) on a poly(styrene-co-maleic acid) (PSMA) surface was investigated by using quartz crystal microbalance (QCM) technique at various pH values. The formation of a BSA surface was examined by atomic force microscopy (AFM). To study the effect on the layer formation, the pH of solution was varied from 2 to 7.4 while the concentration of BSA was in the range of 0.01 to 5 mg/ml during the layer absorption. It was found that the BSA adsorption strongly depends on the pH of solution, and the concentration of BSA. The absorption layer occurred maximum at
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7

Song, Bing, Liwei Yang, Lulu Han, and Lingyun Jia. "Metal Ion-Chelated Tannic Acid Coating for Hemostatic Dressing." Materials 12, no. 11 (2019): 1803. http://dx.doi.org/10.3390/ma12111803.

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Tannic acid (TA), a high-molecular-weight polyphenol, is used as a hemostasis spray and unguent for trauma wound remedy in traditional medical treatment. However, the use of tannic acid on a large-area wound would lead to absorption poisoning. In this work, a TA coating was assembled on a quartz/silicon slide, or medical gauze, via chelation interaction between TA and Fe3+ ions and for further use as a hemostasis dressing. Protein adsorption on the TA coating was further investigated by fluorescence signal, ellipsometry analysis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SD
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8

Reza, Raúl, Carlos Martínez Pérez, Claudia Rodríguez González, Humberto Romero, and Perla García Casillas. "Effect of the polymeric coating over Fe3O4 particles used for magnetic separation." Open Chemistry 8, no. 5 (2010): 1041–46. http://dx.doi.org/10.2478/s11532-010-0073-4.

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AbstractIn this work, the synthesis of magnetite nanoparticles by two variant chemical coprecipitation methods that involve reflux and aging conditions was investigated. The influence of the synthesis conditions on particle size, morphology, magnetic properties and protein adsorption were studied. The synthesized magnetite nanoparticles showed a spherical shape with an average particle size directly influenced by the synthesis technique. Particles of average size 27 nm and 200 nm were obtained. When the coprecipitation method was used without reflux and aging, the smallest particles were obtai
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9

Feng, Hui, Fu-yi Cui, Yi-zhong Xie, Yan Wei, and Zhi-wei Zhao. "Improved efficiency of reactor startup in biological aerated filter by poly(lactic acid)." Water Supply 15, no. 2 (2014): 348–55. http://dx.doi.org/10.2166/ws.2014.120.

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The enhancement effect of polyethylene (PE) surfaces modified with poly(lactic acid) (PLA) on formation of nitrifying biofilms in biological aerated filter (BAF) was investigated in this study. X-ray photoelectron spectroscopy, scanning electron microscope, and protein absorption analysis revealed that modified PE surfaces produced active groups, including carboxyl (O═C─O), hydroxyl (C─OH), and carbonyl (C═O), increased surface roughness, and enhanced the adsorption of both the bovine serum albumin and fibrinogen. During the startup period of 33 days, the average removal rates of ammonia nitro
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10

Rabe, Martin, Andreas Kerth, Alfred Blume, and Patrick Garidel. "Albumin displacement at the air–water interface by Tween (Polysorbate) surfactants." European Biophysics Journal 49, no. 7 (2020): 533–47. http://dx.doi.org/10.1007/s00249-020-01459-4.

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AbstractTween (polysorbate) 20 and 80 are surfactants used for the development of parenteral protein drugs, due to their beneficial safety profile and stabilisation properties. To elucidate the mechanism by which Tween 20 and 80 stabilise proteins in aqueous solutions, either by a “direct” protein to surfactant interaction and/or by an interaction with the protein film at the air–water interface, we used spectroscopic (Infrared Reflection Absorption Spectroscopy, IRRAS) and microscopic techniques (Brewster Angle Microscopy, BAM) in combination with surface pressure measurements. To this end, t
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11

Pradier, C. M., F. Kármán, J. Telegdi, E. Kálmán, and P. Marcus. "Adsorption of Bovine Serum Albumin on Chromium and Molybdenum Surfaces Investigated by Fourier-Transform Infrared Reflection−Absorption Spectroscopy (FT-IRRAS) and X-ray Photoelectron Spectroscopy." Journal of Physical Chemistry B 107, no. 28 (2003): 6766–73. http://dx.doi.org/10.1021/jp026365i.

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12

Fujiwara, Kunio, Masashi Shin, Tsubasa Miyazaki, and Yasuhiro Maruta. "Immunocytochemistry for Amoxicillin and Its Use for Studying Uptake of the Drug in the Intestine, Liver, and Kidney of Rats." Antimicrobial Agents and Chemotherapy 55, no. 1 (2010): 62–71. http://dx.doi.org/10.1128/aac.01031-10.

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ABSTRACTSpecific transport systems for penicillins have been recognized, but theirin vivorole in the context of other transporters remains unclear. We produced a serum against amoxicillin (anti-AMPC) conjugated to albumin with glutaraldehyde. The antiserum was specific for AMPC and ampicillin (ABPC) but cross-reacted weakly with cephalexin. This enabled us to develop an immunocytochemical (ICC) method for detecting the uptake of AMPC in the rat intestine, liver, and kidney. Three hours after a single oral administration of AMPC, the ICC method revealed that AMPC distributed to a high degree in
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13

Giacomelli, Carla E., Marcelo J. Avena, and Carlos P. De Pauli. "Adsorption of Bovine Serum Albumin onto TiO2Particles." Journal of Colloid and Interface Science 188, no. 2 (1997): 387–95. http://dx.doi.org/10.1006/jcis.1996.4750.

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14

Fitzpatrick, H., P. F. Luckham, S. Eriksen, and K. Hammond. "Bovine serum albumin adsorption to mica surfaces." Colloids and Surfaces 65, no. 1 (1992): 43–49. http://dx.doi.org/10.1016/0166-6622(92)80173-y.

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15

Wassell, Diana T. Hughes, Rachel C. Hall, and Graham Embery. "Adsorption of bovine serum albumin onto hydroxyapatite." Biomaterials 16, no. 9 (1995): 697–702. http://dx.doi.org/10.1016/0142-9612(95)99697-k.

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16

Matsukata, Miki, Masahiko Nishino, Jiang Ping Gong, Yoshihito Osada, Yasuhisa Sakurai, and Teruo Okano. "Adsorption of bovine serum albumin to yeast protoplast." Colloids and Surfaces B: Biointerfaces 13, no. 4 (1999): 203–11. http://dx.doi.org/10.1016/s0927-7765(99)00006-5.

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17

Kurrat, Roger, Jeremy J. Ramsden, and Jiri E. Prenosil. "Kinetic model for serum albumin adsorption : experimental verification." Journal of the Chemical Society, Faraday Transactions 90, no. 4 (1994): 587. http://dx.doi.org/10.1039/ft9949000587.

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18

Denkbas, Emir Baki, Mehmet Odabasi, Ebru Kiliçay, and Nalan Özdemir. "Human serum albumin (HSA) adsorption with chitosan microspheres." Journal of Applied Polymer Science 86, no. 12 (2002): 3035–39. http://dx.doi.org/10.1002/app.11318.

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19

Law, S. L., W. Y. Lo, S. H. Pai, G. W. Teh, and F. Y. Kou. "The adsorption of bovine serum albumin by liposomes." International Journal of Pharmaceutics 32, no. 2-3 (1986): 237–41. http://dx.doi.org/10.1016/0378-5173(86)90184-5.

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20

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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21

Seredych, Mykola, Lyuba Mikhalovska, Sergey Mikhalovsky, and Yury Gogotsi. "Adsorption of Bovine Serum Albumin on Carbon-Based Materials." C 4, no. 1 (2018): 3. http://dx.doi.org/10.3390/c4010003.

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22

Wang, Wenjing, Lei Chen, Yipeng Zhang, and Guocheng Liu. "Adsorption of bovine serum albumin and urease by biochar." IOP Conference Series: Earth and Environmental Science 61 (April 2017): 012143. http://dx.doi.org/10.1088/1755-1315/61/1/012143.

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23

Karlsson, L. M., P. Tengvall, I. Lundström, and H. Arwin. "Adsorption of human serum albumin in porous silicon gradients." physica status solidi (a) 197, no. 2 (2003): 326–30. http://dx.doi.org/10.1002/pssa.200306518.

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24

Filisko, Frank E., Devi Malladi, and Sumner Barenberg. "Character of adsorbed bovine serum albumin from adsorption enthalpies." Biomaterials 7, no. 5 (1986): 348–53. http://dx.doi.org/10.1016/0142-9612(86)90005-0.

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25

Tay, L., N. L. Rowell, D. Poitras, J. W. Fraser, D. J. Lockwood, and R. Boukherroub. "Bovine serum albumin adsorption on passivated porous silicon layers." Canadian Journal of Chemistry 82, no. 10 (2004): 1545–53. http://dx.doi.org/10.1139/v04-129.

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Hydrogen-terminated porous silicon (pSi-H) films were fabricated through electrochemical anodization of crystalline silicon in hydrofluoric-acid-based solutions. The pSi-H surface was chemically functionalized by thermal reaction with undecylenic acid to produce an organic monolayer covalently attached to the silicon surface through Si—C bonds and bearing an acid terminal group. Bovine serum albumin (BSA) was adsorbed onto such surface-modified pSi structures. The resulting surfaces were characterized using scanning electron microscopy (SEM), reflection FT-IR spectroscopy, and ellipsometry. SE
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26

Modarress, Hamid, and Mohsen Mohsen-Nia. "Experimental study of bovine serum albumin adsorption onto hydroxylapatite." Journal of Biotechnology 131, no. 2 (2007): S254—S255. http://dx.doi.org/10.1016/j.jbiotec.2007.07.460.

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27

Fukuzaki, Satoshi, Hiromi Urano, and Kazuya Nagata. "Adsorption of bovine serum albumin onto metal oxide surfaces." Journal of Fermentation and Bioengineering 81, no. 2 (1996): 163–67. http://dx.doi.org/10.1016/0922-338x(96)87596-9.

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28

Gallinet, Jean-Paul, and Bernard Gauthier-Manuel. "Adsorption—desorption of serum albumin on bare mica surfaces." Colloids and Surfaces 68, no. 3 (1992): 189–93. http://dx.doi.org/10.1016/0166-6622(92)80203-e.

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29

Leibner, Evan S., Naris Barnthip, Weinan Chen, et al. "Superhydrophobic effect on the adsorption of human serum albumin." Acta Biomaterialia 5, no. 5 (2009): 1389–98. http://dx.doi.org/10.1016/j.actbio.2008.11.003.

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30

Vanýsek, Petr, and Zhisheng Sun. "Bovine serum albumin adsorption on a water / nitrobenzene interface." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 298, no. 2 (1990): 177–94. http://dx.doi.org/10.1016/0022-0728(90)87461-r.

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31

Vanýsek, Petr, and Zhisheng Sun. "Bovine serum albumin adsorption on a water/nitrobenzene interface." Bioelectrochemistry and Bioenergetics 23, no. 2 (1990): 177–94. http://dx.doi.org/10.1016/0302-4598(90)85007-5.

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32

Wassell, Diana T. Hughes, and Graham Embery. "Adsorption of bovine serum albumin on to titanium powder." Biomaterials 17, no. 9 (1996): 859–64. http://dx.doi.org/10.1016/0142-9612(96)83280-7.

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33

Peng, Z. G., K. Hidajat, and M. S. Uddin. "Adsorption of bovine serum albumin on nanosized magnetic particles." Journal of Colloid and Interface Science 271, no. 2 (2004): 277–83. http://dx.doi.org/10.1016/j.jcis.2003.12.022.

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34

McClellan, Scott J., and Elias I. Franses. "Adsorption of bovine serum albumin at solid/aqueous interfaces." Colloids and Surfaces A: Physicochemical and Engineering Aspects 260, no. 1-3 (2005): 265–75. http://dx.doi.org/10.1016/j.colsurfa.2005.03.017.

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35

Matsuhisa, Shigeki, Shingo Takesawa, and Kiyotaka Sakai. "Binary-solute adsorption of dosed drugs on serum albumin." Chemical Engineering Journal 34, no. 2 (1987): B21—B27. http://dx.doi.org/10.1016/0300-9467(87)87009-0.

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36

Douillard, Roger. "Adsorption of serum albumin at the oil/water interface." Colloids and Surfaces A: Physicochemical and Engineering Aspects 91 (November 1994): 113–19. http://dx.doi.org/10.1016/0927-7757(94)02764-1.

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37

Lin, Yeong-Shang, and Vladimir Hlady. "Human serum albumin adsorption onto octadecyldimethylsilyl-silica gradient surface." Colloids and Surfaces B: Biointerfaces 2, no. 5 (1994): 481–91. http://dx.doi.org/10.1016/0927-7765(94)80056-1.

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38

Bolton, Barbara A., and James R. Scherer. "Raman spectra and water absorption of bovine serum albumin." Journal of Physical Chemistry 93, no. 22 (1989): 7635–40. http://dx.doi.org/10.1021/j100359a021.

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39

Kizuki, Takashi, Takao Saito, Masataka Ohgaki, and Yoshiyuki Yokogawa. "Effects of Serum Proteins in Apatite Layer Formed in Culture Medium on Initial Adhesion and Cell Proliferation." Key Engineering Materials 309-311 (May 2006): 283–88. http://dx.doi.org/10.4028/www.scientific.net/kem.309-311.283.

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In cell culture medium containing serum proteins, a layer with a great role in ostelblast-like cell’s growth formed on a HAp ceramics by a coprecipitation with a deposition of a bone-like apatite and an adsorption of serum proteins. The adsorption of proteins is influential in the apatite deposition and the cell adhesion. A component of serum albumin is forming < 80% of total serum proteins, therefore we focused on the serum albumin. The serum albumin was removed from fetal bovine serum by using an albumin removal kit, and then the albumin free cell culture medium was prepared. The bone-lik
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40

Wang, Linghe, Lijie Qiao, and Yu Yan. "Adsorption of bovine serum albumin and nanocrystallines on biomedical alloys." Bioinspired, Biomimetic and Nanobiomaterials 6, no. 1 (2017): 12–19. http://dx.doi.org/10.1680/jbibn.16.00026.

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41

Chen-Hua, ZHU, SHEN He-Bai, XU Rui-Yun, WANG Hao-Yue, and HAN Ji-Mei. "The Adsorption of Bovine Serum Albumin onto Magnetic Chitosan Microspheres." Acta Physico-Chimica Sinica 23, no. 10 (2007): 1583–88. http://dx.doi.org/10.3866/pku.whxb20071017.

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42

Niyomthai, Saowapa T., Prasit Pavasant, and Pitt Supaphol. "Adsorption study of bovine serum albumin onto multiwalled carbon nanotubes." Materials Today: Proceedings 33 (2020): 1814–18. http://dx.doi.org/10.1016/j.matpr.2020.05.060.

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43

Wu, Qi-Ci, Qi-Lei Zhang, Dong Gao, et al. "Mixed-Mode Expanded-Bed Adsorption for Human Serum Albumin Separation." Industrial & Engineering Chemistry Research 57, no. 3 (2018): 1039–47. http://dx.doi.org/10.1021/acs.iecr.7b03799.

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44

Mondal, Subrata, Cunben Li, and Kean Wang. "Bovine Serum Albumin Adsorption on Gluteraldehyde Cross-Linked Chitosan Hydrogels." Journal of Chemical & Engineering Data 60, no. 8 (2015): 2356–62. http://dx.doi.org/10.1021/acs.jced.5b00264.

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45

Feng, B., J. Weng, B. C. Yang, et al. "Surface characterization of titanium and adsorption of bovine serum albumin." Materials Characterization 49, no. 2 (2002): 129–37. http://dx.doi.org/10.1016/s1044-5803(02)00341-8.

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46

Shi, Jie, Bo Feng, Xiong Lu, and Jie Weng. "Adsorption of bovine serum albumin onto titanium dioxide nanotube arrays." International Journal of Materials Research 103, no. 7 (2012): 889–96. http://dx.doi.org/10.3139/146.110696.

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47

Karada??, Erdener, Dursun Saraydin, H. Nursevin Öztop, and Olgun Güven. "Adsorption of bovine serum albumin to acrylamide–itaconic acid hydrogels." Polymers for Advanced Technologies 5, no. 10 (1994): 664–68. http://dx.doi.org/10.1002/pat.1994.220051006.

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48

Lenk, Thomas J., Buddy D. Ratner, R. Michael Gendreau, and Krishnan K. Chittur. "IR spectral changes of bovine serum albumin upon surface adsorption." Journal of Biomedical Materials Research 23, no. 6 (1989): 549–69. http://dx.doi.org/10.1002/jbm.820230603.

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49

Du, Jennifer Runhong, Xiao Su, and Xianshe Feng. "Chitosan/sericin blend membranes for adsorption of bovine serum albumin." Canadian Journal of Chemical Engineering 95, no. 5 (2017): 954–60. http://dx.doi.org/10.1002/cjce.22760.

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50

Kandori, Kazuhiko, Miwa Saito, Taro Takebe, Akemi Yasukawa, and Tatsuo Ishikawa. "Adsorption of Bovine Serum Albumin on Synthetic Carbonate Calcium Hydroxyapatite." Journal of Colloid and Interface Science 174, no. 1 (1995): 124–29. http://dx.doi.org/10.1006/jcis.1995.1373.

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