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 contained in culture medium used in artificial insemination is an important anaphylaxis risk factor

2008 ◽  
Vol 90 (5) ◽  
pp. 2013.e17-2013.e19 ◽  
Author(s):  
Juan A. Pagán ◽  
Idoia Postigo ◽  
Jorge R. Rodríguez-Pacheco ◽  
Maribel Peña ◽  
Jorge A. Guisantes ◽  
...  
Keyword(s):  
Risk Factor ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Artificial Insemination ◽  
Bovine Serum ◽  
Culture Medium

Thiol-reactive Clenbuterol Analogues Conjugated to Bovine Serum Albumin

2004 ◽  
Vol 59 (11-12) ◽  
pp. 880-886 ◽  
Author(s):  
Marko Oblak ◽  
Andrej Preželj ◽  
Slavko Pečar ◽  
Tom Solmajer
Keyword(s):  
Molecular Dynamics ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Spin Label ◽  
Bovine Serum ◽  
Spin Probe ◽  
Coupling Reaction ◽  
High Yield ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

Several novel thiol-reactive clenbuterol analogues were coupled in high yield with bovine serum albumin (BSA). After labelling of unreacted cysteines with maleimide spin label (MiSL), the yield of the coupling reaction was determined by electron paramagnetic resonance (EPR) spectroscopy and spectral analysis. Two spin-probe populations with different mobility states were quantitatively determined. Molecular dynamics was used to model the structure of clenbuterol analogues and spin label conjugated to BSA and recognition of conjugates by anti-clenbuterol antibodies was demonstrated. The recognition of BSA-A, BSA-C and BSAS conjugates with monoclonal and polyclonal anti-clenbuterol (mCLB-Ab and rCLB-Ab) antibodies was an indication, that chlorine substituents on the aromatic ring of clenbuterol derivatives are not necessary for the binding of antibodies to the conjugates. These results confirmed the importance of the tert-butylamino group as a part of the epitope and contribute to the understanding of the recognition process with anti-clenbuterol antibodies.

Successful Reversal of Diabetes by Single Donor Isologous Islet Transplantation in a Mouse Model

1997 ◽  
Vol 6 (4) ◽  
pp. 429-430 ◽  
Author(s):  
C. K. Leow ◽  
D. W. R. Gray ◽  
P. J. Morris
Keyword(s):  
Bovine Serum Albumin ◽  
Mouse Model ◽  
Serum Albumin ◽  
Islet Transplantation ◽  
Bovine Serum ◽  
High Yield ◽  
Renal Capsule ◽  
Single Donor ◽  
Mouse Islets ◽  
The Mean

A method for isolating mouse islets which consistently gives a high yield with good purity is described. Using a bovine serum albumin gradient, the mean yield of islets per pancreas is 425 (SEM ± 15) with a consistent purity of over 90%. Single donor to single recipient of islets transplanted under the renal capsule restores normoglycemia in the diabetic recipients within 2 to 5 days of transplantation.

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.

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.

scholarly journals PS48 can replace bovine serum albumin in pig embryo culture medium, and improve in vitro embryo development by phosphorylating AKT

2015 ◽  
Vol 82 (4) ◽  
pp. 315-320 ◽  
Author(s):  
Lee D. Spate ◽  
Alana Brown ◽  
Bethany K. Redel ◽  
Kristin M. Whitworth ◽  
Randall S. Prather
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Embryo Development ◽  
Embryo Culture ◽  
Bovine Serum ◽  
Culture Medium ◽  
Embryo Culture Medium

Generation of Factor VIII:C by Isolated Pig and Rat Livers

1979 ◽  
Author(s):  
C. A. Owen ◽  
E. J. Walter Bowie ◽  
D. N. Fass
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rat Plasma ◽  
Rat Erythrocytes ◽  
Adult Rat ◽  
Coagulant Activity ◽  
Neonatal Pig ◽  
Willebrand Factor ◽  
Rat Livers

When isolated neonatal pig livers were perfused with blood from pigs with von Wille-brand’s disease, no factor VIII coagulant activity (VIII.C) emerged in the perfusate. When purified porcine Willebrand factor, lacking VIII:C, was added to the perfusate it rapidly diminished, presumably being taken up by the liver. Concurrently VIII:C rose steadily in the blood during the 5 hours of perfusion. Similarly, isolated adult rat livers released no VIII:C when they were perfused with rat erythrocytes suspended in Tyrode’s solution containing 6% bovine serum albumin. VIII:C did emcrRe if cryoprecipitate from aged rat plasma were added. The neo-VIII:C was rapidly inactivated by plasma from a patient with classic hemophilia who had developed an antibody to VIII:C. Addition of cycloheximide to the rat before extirpation of the liver, as well as to the perfusate, prevented the emergence of VIII:C. We suspect that VIII:C is derived from the liver but only when Willebrand factor is present.

scholarly journals Optimization of nano-encapsulation on neonatal porcine islet-like cell clusters using polymersomes

2020 ◽  
Author(s):  
Sang Hoon Lee ◽  
Hyun-Ouk Kim ◽  
Jung-Taek Kang
Keyword(s):  
Extracellular Matrix ◽  
Polyethylene Glycol ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Culture Medium ◽  
Cell Clusters ◽  
Porcine Islet ◽  
Minimal Damage ◽  
Amine Groups

Abstract ObjectiveResearches proving methods for nano encapsulation of neonatal porcine islet-like cell clusters (NPCCs) using polymersomes (PSomes) formed using polymers of polyethylene glycol-block-poly lactide (PEG-b-PLA). Herein, our studies present efficient nano encapsulation procedure with minimal damage and loss of NPCCs. MethodsWe used N-hydroxysuccinimide (NHS) on the N-terminal of PSomes to induce binding of amine groups in the extracellular matrix surrounding NPCCs. F-10 culture medium with bovine serum albumin was used in the nano-encapsulation procedure to minimize damage and loss of NPCCs. Finally, we induced crosslinking between bi-functional PSomes (NHS-/NH2-PSomes). ResultsF-10 culture medium containing 0.25% BSA with pH of 7.3 minimized the damage and loss of NPCCs after nano-encapsulation as compared with using basic HBSS buffer (pH 8.0). Also, we induced the efficiency nano encapsulation through conjugation of PSomes using bi-functional PSomes (NHS-/NH2-PSomes).

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