Studies on the Adsorption and Thermodynamics of Theophylline, Vitamin C and Bovine Serum Albumin on Microporous Corn Starch

2018 ◽  
Vol 71 (3-4) ◽  
pp. 1800042
Author(s):  
Yuhua Li ◽  
Yeli Zhang ◽  
Juan Zhao ◽  
Ning Han ◽  
Liujiao Bian
Keyword(s):  
Bovine Serum Albumin ◽  
Vitamin C ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Corn Starch

Interaction of aspirin and vitamin C with bovine serum albumin

2011 ◽  
Vol 105 (3) ◽  
pp. 198-202 ◽  
Author(s):  
Shohreh Nafisi ◽  
Golshan Bagheri Sadeghi ◽  
Ataollah PanahYab
Keyword(s):  
Bovine Serum Albumin ◽  
Vitamin C ◽  
Serum Albumin ◽  
Bovine Serum

Lag phase alteration in the modified bovine serum albumin under the inducing and inhibitory effect of vitamin C

2018 ◽  
Vol 15 (6) ◽  
pp. 1337-1346
Author(s):  
E. Vahdat-Ahar ◽  
A. A. Moosavi-Movahedi ◽  
F. Taghavi ◽  
M. Habibi-Rezaei ◽  
N. Sheibani
Keyword(s):  
Bovine Serum Albumin ◽  
Vitamin C ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Inhibitory Effect ◽  
Lag Phase

Spectroscopic Studies on the Interaction of Vitamin C with Bovine Serum Albumin

2008 ◽  
Vol 38 (1) ◽  
pp. 15-25 ◽  
Author(s):  
Hui Xu ◽  
Quanwen Liu ◽  
Ying Zuo ◽  
Yan Bi ◽  
Shuli Gao
Keyword(s):  
Bovine Serum Albumin ◽  
Vitamin C ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies

scholarly journals Radioprotective Role of Vitamins C and E against the Gamma Ray-Induced Damage to the Chemical Structure of Bovine Serum Albumin

Antioxidants ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1875
Author(s):  
Hajar Zarei ◽  
Mostean Bahreinipour ◽  
Yahya Sefidbakht ◽  
Shokouh Rezaei ◽  
Rouhollah Gheisari ◽  
...  
Keyword(s):  
Vitamin E ◽  
Bovine Serum Albumin ◽  
Vitamin C ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Structural Changes ◽  
Gamma Ray ◽  
Fluorescence Emission ◽  
Water Soluble ◽  
Radiation Induced

Radioprotective effects of vitamin C and vitamin E as a water-soluble and a lipid-soluble agent, respectively, were investigated at the molecular level during the imposition of gamma radiation-induced structural changes to bovine serum albumin (BSA) at the therapeutic dose of 3 Gy. Secondary and tertiary structural changes of control and irradiated BSA samples were investigated using circular dichroism and fluorescence spectroscopy. The preirradiation tests showed nonspecific and reversible binding of vitamins C and E to BSA. Secondary and tertiary structures of irradiated BSA considerably changed in the absence of the vitamins. Upon irradiation, α-helices of BSA transitioned to beta motifs and random coils, and the fluorescence emission intensity decreased relative to nonirradiated BSA. In the presence of the vitamins C or E, however, the irradiated BSA was protected from these structural changes caused by reactive oxygen species (ROS). The two vitamins exhibited different patterns of attachment to the protein surface, as inspected by blind docking, and their mechanisms of protection were different. The hydrophilicity of vitamin C resulted in the predominant scavenging of ROS in the solvent, whereas hydrophobic vitamin E localized on the nonpolar patches of the BSA surface, where it did not only form a barrier for diffusing ROS but also encountered them as an antioxidant and neutralized them thanks to the moderate BSA binding constant. Very low concentrations of vitamins C or E (0.005 mg/mL) appear to be sufficient to prevent the oxidative damage of BSA.

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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