Intercalation of Bovine Serum Albumin Coated Gold Clusters Between Phospholipid Bilayers: Temperature-Dependent Behavior of Lipid-AuQC@BSA Assemblies with Red Emission and Superlattice Structure

2014 ◽  
Vol 118 (14) ◽  
pp. 3887-3892 ◽  
Author(s):  
Balázs Söptei ◽  
Judith Mihály ◽  
Júlia Visy ◽  
András Wacha ◽  
Attila Bóta
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Gold Clusters ◽  
Phospholipid Bilayers ◽  
Temperature Dependent ◽  
Red Emission ◽  
Superlattice Structure ◽  
Dependent Behavior ◽  
Temperature Dependent Behavior

Ratiometric fluorescent probe based on novel red-emission BODIPY for determination of bovine serum albumin

2014 ◽  
Vol 30 (5) ◽  
pp. 738-742 ◽  
Author(s):  
Fengling Song ◽  
Yingying Xue ◽  
Xu Wang ◽  
Jingyun Wang ◽  
Xiaoqing Xiong ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescent Probe ◽  
Bovine Serum ◽  
Red Emission ◽  
Ratiometric Fluorescent Probe

Antimutagenic activity of whole casein on the pepper-induced mutagenicity to streptomycin-dependent strain SD 510 of Salmonella typhimurium TA 98

1988 ◽  
Vol 55 (3) ◽  
pp. 435-442 ◽  
Author(s):  
Akiyoshi Hosono ◽  
Kunigal N. Shashikanth ◽  
Hajime Otani
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Salmonella Typhimurium ◽  
Bovine Serum ◽  
Trypsin Digestion ◽  
Antimutagenic Activity ◽  
Temperature Dependent ◽  
Egg Albumin ◽  
Dependent Strain ◽  
Papain Digestion

SummaryWhen the antimutagenic activity of milk or cultured milk components on the pepper-induced mutagenicity to streptomycin-dependent strain SD 510 of Salmonella typhimurium TA 98 was investigated, whole casein showed a significant antimutagenic activity. Heating at 121 °C for 15 min completely destroyed the antimutagenic activity of casein, which was temperature dependent. While acid or papain digestion resulted in the loss of antimutagenic activity of casein, trypsin digestion had little effect although the digestion of casein by each proteinase was over 75%. β-Casein, egg albumin, and bovine serum albumin also had a similar antimutagenic activity to that of whole casein.

Thermo-reversibility, ergodicity and surface charge–temperature dependent phase diagram of anionic, cationic and neutral co-gels of gelatin–BSA complexes

RSC Advances ◽  
2016 ◽  
Vol 6 (46) ◽  
pp. 40123-40136 ◽  
Author(s):  
Jyotsana Pathak ◽  
Kamla Rawat ◽  
H. B. Bohidar
Keyword(s):  
Phase Diagram ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Mixing Ratio ◽  
Temperature Dependent ◽  
Gelation Behavior ◽  
Ph Range ◽  
Protein Bovine Serum Albumin ◽  
Charge Temperature

We have investigated the gelation behavior of polyampholyte gelatin B (GB) in the presence of colloidal plasma protein bovine serum albumin (BSA) as a function of mixing ratio (r = GB : BSA = 1.5–4), entire pH range, and temperature (20–45 °​C).

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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