Osmotic susceptibility and diffusion coefficient of charged bovine serum albumin

1984 ◽  
Vol 80 (7) ◽  
pp. 3469-3477 ◽  
Author(s):  
Dennis G. Neal ◽  
Daniel Purich ◽  
David S. Cannell
Keyword(s):  
Diffusion Coefficient ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
And Diffusion

Interaction and diffusion of gold nanoparticles in bovine serum albumin solutions

2013 ◽  
Vol 102 (20) ◽  
pp. 203705 ◽  
Author(s):  
Indermeet Kohli ◽  
Sharmine Alam ◽  
Bhavdeep Patel ◽  
Ashis Mukhopadhyay
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
And Diffusion

scholarly journals Concentration dependence of translational diffusion coefficients for globular proteins

The Analyst ◽  
2014 ◽  
Vol 139 (23) ◽  
pp. 6242-6248 ◽  
Author(s):  
David J. Scott ◽  
Stephen E. Harding ◽  
Donald J. Winzor
Keyword(s):  
Diffusion Coefficient ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diffusion Coefficients ◽  
Bovine Serum ◽  
Globular Proteins ◽  
Sedimentation Velocity ◽  
Translational Diffusion ◽  
Translational Diffusion Coefficient ◽  
Reasonable Approximation

This investigation examines published results of traditional diffusion experiments on ovalbumin and bovine serum albumin to determine the extent to which assumed concentration independence of the translational diffusion coefficient is a reasonable approximation in the analysis of boundary spreading in sedimentation velocity experiments on proteins.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

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