scholarly journals Influence of bovine serum albumin on corrosion behaviour of pure Zn in phosphate buffered saline

2021 ◽  
Vol 32 (9) ◽  
Author(s):  
Lijun Liu ◽  
Lili Lu ◽  
Hai-Jun Zhang ◽  
Lu-Ning Wang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Corrosion Behaviour ◽  
Electrochemical Techniques ◽  
Material Surface ◽  
Biodegradable Metals ◽  
Phosphate Buffered Saline ◽  
Stent Material ◽  
Bsa Adsorption

AbstractZinc (Zn) and its alloys have received increasing attention as new alternative biodegradable metals. However, consensus has not been reached on the corrosion behaviour of Zn. As cardiovascular artery stent material, Zn is supposed to contact with plasma that contains inorganic salts and organic components. Protein is one of the most important constitute in the plasma and could adsorb on the material surface. In this paper, bovine serum albumin (BSA) was used as a typical protein. Influences of BSA on pure Zn corrosion in phosphate buffered saline is investigated as a function of BSA concentrations and immersion durations by electrochemical techniques and surface analysis. Results showed that pure Zn corrosion was progressively accelerated with BSA concentrations (ranging from 0.05 to 5 g L−1) at 0.5 h. With time evolves, formation of phosphates as corrosion product was delayed by BSA adsorption, especially at concentration of 2 g L−1. Within 48 h, the corrosion of pure Zn was alleviated by BSA at concentration of 0.1 g L−1, whereas the corrosion was enhanced after 168 h. Addition of 2 g L−1 BSA has opposite influence on the pure Zn corrosion. Furthermore, schematic corrosion behaviour at protein/Zn interfaces was proposed. This work encourages us to think more about the influence of protein on the material corrosion and helps us to better understand the corrosion behaviour of pure Zn.

BSA Adsorption on Hydroxyapatite after Thermal Treatment

2007 ◽  
Vol 361-363 ◽  
pp. 127-130 ◽  
Author(s):  
Elena Mavropoulos ◽  
Nilce C.C. da Rocha ◽  
Maria Helena M. Rocha-Leão ◽  
Antonella M. Rossi
Keyword(s):  
Thermal Treatment ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Active Sites ◽  
Sorption Process ◽  
Buffer Concentration ◽  
Surface Active ◽  
Bsa Adsorption

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.

A Method of Obtaining a Suspension of Intact Parenchymal Cells from Adult Rat Liver

1971 ◽  
Vol 8 (1) ◽  
pp. 73-86
Author(s):  
JENNIFER J. GALLAI-HATCHARD ◽  
G. M. GRAY
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Culture Medium ◽  
High Yield ◽  
Alkaline Ph ◽  
High Osmolarity ◽  
Adult Rat ◽  
Parenchymal Cells ◽  
Phosphate Buffered Saline

The perfusion of liver with either citrate or tetraphenyl boron to remove Ca2+ or K+ or with a solution of high osmolarity and alkaline pH yields plenty of cells but they are all damaged. Perfusion of the liver with hyaluronidase and collagenase followed by incubation of liver slices in the same enzyme solution produced a high yield of cells (25%, w/w, of liver) of which only about 1% were undamaged. However, perfusion with 0.3% hyaluronidase, 0.3% collagenase and 0.1% trypsin in phosphate-buffered saline (excluding Mg2+ and Ca2+) followed by incubation at 25 °C of the chopped liver gave a small yield (2-4%, w/w) of undamaged cells which were not permeable to eosin for up to an hour when suspended in culture medium containing 2% bovine serum albumin.

Bovine serum albumin adsorption on passivated porous silicon layers

2004 ◽  
Vol 82 (10) ◽  
pp. 1545-1553 ◽  
Author(s):  
L Tay ◽  
N L Rowell ◽  
D Poitras ◽  
J W Fraser ◽  
D J Lockwood ◽  
...  
Keyword(s):  
Porous Silicon ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Crystalline Silicon ◽  
Electrochemical Anodization ◽  
Undecylenic Acid ◽  
Ft Ir ◽  
Lift Off ◽  
Bsa Adsorption

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. SEM showed that the porous films were damaged and partially lifted off the silicon substrate after a prolonged BSA adsorption. Ellipsometry analysis revealed that the BSA penetrated ∼1.3 µm into the porous structure. The film damage is likely a result of BSA anchoring itself tightly through strong electrostatic interaction with the acid-covered Si sidewalls. A change in surface tension during BSA film formation then causes the pSi layer to buckle and lift off the underlying Si substrate. FT-IR results from the undecylenic-acid-modified pSi surfaces before and after BSA adsorption showed the presence of strong characteristic amide I, II, and III vibrational bands after BSA adsorption. The surface properties of the pSi matrix and its interactions with BSA are examined in this study.Key words: ellipsometry, porous silicon, protein adsorption, surface passivation.

scholarly journals Deuteroporphyrin-albumin binding equilibrium. The effects of porphyrin self-aggregation studied for the human and the bovine proteins

1985 ◽  
Vol 229 (1) ◽  
pp. 197-203 ◽  
Author(s):  
M Rotenberg ◽  
R Margalit
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Competitive Model ◽  
Phosphate Buffered Saline ◽  
Self Aggregation

The binding equilibrium of deuteroporphyrin IX to human serum albumin and to bovine serum albumin was studied, by monitoring protein-induced changes in the porphyrin fluorescence and taking into consideration the self-aggregation of the porphyrin. To have control over the latter, the range of porphyrin concentrations was chosen to maker dimers (non-covalent) the dominant aggregate. Each protein was found to have one high-affinity site for deuteroporphyrin IX monomers, the magnitudes of the equilibrium binding constants (25 degrees C, neutral pH, phosphate-buffered saline) being 4.5 (+/- 1.5) X 10(7) M-1 and 1.7 (+/- 0.2) X 10(6) M-1 for human serum albumin and for bovine serum albumin respectively. Deuteroporphyrin IX dimers were found to bind directly to the protein, each protein binding one dimer, with high affinity. Two models are proposed for the protein-binding of porphyrin monomers and dimers in a porphyrin system having both species: a competitive model, where each protein molecule has only one binding site, which can be occupied by either a monomer or a dimer; a non-competitive model, where each protein molecule has two binding sites, one for monomers and one for dimers. On testing the fit of the data to the models, an argument can be made to favour the non-competitive model, the equilibrium binding constants of the dimers, for the non-competitive model (25 degrees C, neutral pH, phosphate-buffered saline), being: 8.0 (+/- 1.8) X 10(8) M-1 and 1.2 (+/- 0.6) X 10(7) M-1 for human serum albumin and bovine serum albumin respectively.

Selection of a surrogate matrix for the quantification of an endogenous analyte in dried whole blood

Bioanalysis ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 409-418 ◽  
Author(s):  
Amy E Leaney ◽  
Carl Horner ◽  
Philip B Grace ◽  
Deborah H Mawson
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Whole Blood ◽  
Bovine Serum ◽  
Hydroxyvitamin D ◽  
Assay Performance ◽  
25 Hydroxyvitamin D ◽  
Surrogate Matrix ◽  
Phosphate Buffered Saline ◽  
Selection Of

Aim: A surrogate matrix is needed to quantify 25-hydroxyvitamin D3 in dried whole blood (DWB). To date, there has been limited guidance on approaches for quantification of endogenous analytes in atypical matrices, such as DWB. Methods: Different surrogate matrices were investigated in a systematic process using an LC–MS/MS assay. Performance assessment was made using quality controls of DWB with different hematocrits. Results & conclusion: Suitability of both phosphate-buffered saline containing bovine serum albumin and washed red blood cells recombined with phosphate-buffered saline containing bovine serum albumin as a surrogate matrix was demonstrated across a range of concentrations and hematocrits representative of expected endogenous analyte samples.

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