Hierarchical Surface Charge Dependent Phase States of Gelatin–Bovine Serum Albumin Dispersions Close to Their Common pI

2014 ◽  
Vol 118 (38) ◽  
pp. 11161-11171 ◽  
Author(s):  
Jyotsana Pathak ◽  
Kamla Rawat ◽  
V. K. Aswal ◽  
H. B. Bohidar
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Charge ◽  
Bovine Serum

Effect of surface charge on adsorption of bovine serum albumin as studied by ellipsometry 1. Adsorption on cationic monolayer

1986 ◽  
Vol 264 (10) ◽  
pp. 903-908 ◽  
Author(s):  
N. Watanabe ◽  
T. Shirakawa ◽  
M. Iwahashi ◽  
K. Ohbu ◽  
T. Seimiya
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Charge ◽  
Bovine Serum ◽  
Effect Of Surface

Contribution of Surface Charge to Bovine Serum Albumin Adsorption on Hydroxyapatite Ceramic Particles

2007 ◽  
Vol 330-332 ◽  
pp. 861-864 ◽  
Author(s):  
Xiang Dong Zhu ◽  
Hong Song Fan ◽  
X. N. Chen ◽  
Dong Xiao Li ◽  
Xing Dong Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Charge ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Solid Particles ◽  
Hydroxyapatite Ceramic ◽  
Liquid Environment ◽  
Zeta Potentials ◽  
Albumin Adsorption

Protein adsorption is driven by various interactions. The contribution of surface charge to bovine serum albumin (BSA) adsorption on hydroxyapatite (HA) ceramic was investigated by adjusting the liquid environment in which the solid particles dispersed. Zeta potentials of HA and the adsorption of BSA on the surface were tested as a function of pH, ionic strength, Ca2+ and PO4 3- concentrations in the aqueous solutions, and the results showed that both of them were greatly affected by those experimental variations. Besides, the amount of adsorbed BSA was related to the variation of zeta potential of HA, as could be well understood in terms of electrostatic interactions.

scholarly journals Fluorescent Fatty Acid Transfer from Bovine Serum Albumin to Phospholipid Vesicles: Collision or Diffusion Mediated Uptake

2012 ◽  
Vol 15 (3) ◽  
pp. 420 ◽  
Author(s):  
Bassam M Elmadhoun ◽  
Manal A Swairjo ◽  
Frank J Burczynski
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Charge ◽  
Bovine Serum ◽  
Binding Proteins ◽  
Lipid Membrane ◽  
Free Ligand ◽  
Lipid Vesicles ◽  
Extracellular Proteins ◽  
Uptake Process

Purpose: The extent of palmitate uptake by hepatocytes is dependent upon the surface charge of the extracellular binding protein. Specifically, hepatocyte uptake is greater when palmitate is bound to cationic binding proteins than when it is bound to anionic proteins. To further understand the role of protein surface charge on the uptake process of protein-bound ligands, we examined the rate of transfer of fluorescent anthroyloxy palmitic acid (AOPA) in the presence of anionic and cationic extracellular proteins to model membranes containing different surface charged groups. Method: AOPA transfer rate in the presence of bovine serum albumin (ALB; isoelectric point pI = 4.8-5.0) or modified ALB (ALBe; pI = 7.0-7.5) to negative, positive and neutral lipid vesicles was investigated using a fluorescence resonance energy transfer assay. Results: The rate of AOPA transfer from both proteins was decreased when ionic strength was increased; directly dependent on the concentration of acceptor lipid vesicles; and was affected by both the lipid membrane surface charge and protein-bound concentration. Conclusion: The data support the notion that AOPA transfer from binding proteins to lipid membranes occurred through two concomitant processes, aqueous diffusion of the unbound ligand (diffusion-mediated process) and a collisional interaction between the protein-ligand complex and acceptor membrane. The contribution of diffusional mediated transfer to the overall uptake process was determined to be 3 to 4 times less than the contribution of a collisional interaction. This study strengthened the hypothesis that charged amino acid residues on proteins are important for effective collisional interaction between protein-ligand complexes and cell membranes through which more free ligand could be supplied for the uptake process. This article is open to POST-PUBLICATION REVIEW. Registered readers (see “For Readers”) may comment by clicking on ABSTRACT on the issue’s contents page.

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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