Interactions of PAMAM Dendrimers with Bovine Serum Albumin in the Presence of Copper and Iron Ions

2008 ◽  
Author(s):  
Jing-Xian Yu ◽  
Jian-Qun Shao ◽  
Shu-Lian Yan ◽  
Cong-Xia Wang ◽  
Ling Ye
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Pamam Dendrimers ◽  
Iron Ions

Interactions between PAMAM dendrimers and bovine serum albumin

2003 ◽  
Vol 1648 (1-2) ◽  
pp. 115-126 ◽  
Author(s):  
Barbara Klajnert ◽  
Lidia Stanisławska ◽  
Maria Bryszewska ◽  
Bartłomiej Pałecz
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Pamam Dendrimers

Fluorescence study on the interactions of PAMAM dendrimers and their derivatives with bovine serum albumin

2005 ◽  
Vol 50 (21) ◽  
pp. 2436-2441 ◽  
Author(s):  
Yanming Wang ◽  
Yu Song ◽  
Deling Kong ◽  
Yaoting Yu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Pamam Dendrimers ◽  
Fluorescence Study

scholarly journals Is Iron Chelation Important in Preventing Glycation of Bovine Serum Albumin in Vitro?

2015 ◽  
Vol 20 (4) ◽  
Author(s):  
Sabina Galiniak ◽  
Grzegorz Bartosz ◽  
Izabela Sadowska-Bartosz
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Iron Chelation ◽  
Protein Glycation ◽  
Iron Ions ◽  
Metal Chelators ◽  
Proper System

AbstractThe role of metal (especially) iron ions has been postulated to play a prominent role in protein glycation, suggesting antiglycating effectiveness of metal chelators. However, this rule may not apply to all model glycation systems. We found that metal chelators are not effective in prevention of glycation of bovine serum albumin (BSA) in vitro, and there is no correlation between the antiglycating effects of 32 compounds and their iron chelation activity as measured with the ferrozine test. These data indicate that the glycation of BSA in vitro is iron-independent and is not a proper system to study the role of metals in protein glycation.

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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