Studies on the interaction of salicylic acid and its monohydroxy substituted derivatives with bovine serum albumin

2021 ◽  
Vol 546 ◽  
pp. 111182
Author(s):  
Deying Meng ◽  
Huangmei Zhou ◽  
Jianhua Xu ◽  
Sanjun Zhang
Keyword(s):  
Salicylic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Physically crosslinked salicylate-based poly (N-isopropylacrylamide-co-acrylic acid) hydrogels for protein delivery

2017 ◽  
Vol 33 (2) ◽  
pp. 224-236 ◽  
Author(s):  
Bahar Demirdirek ◽  
Kathryn E Uhrich
Keyword(s):  
Salicylic Acid ◽  
Bovine Serum Albumin ◽  
Acrylic Acid ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Delivery ◽  
Temperature Sensitive ◽  
Polymer Systems ◽  
Physical Interactions ◽  
Physically Crosslinked

Physically crosslinked hydrogels were developed via solvent casting methods using a temperature-sensitive polymer, poly( N-isopropylacrylamide- co-acrylic acid), and a therapeutic polymer, salicylate-based poly(anhydride-esters), to concurrently release salicylic acid and bovine serum albumin in a sustained manner. The physical interactions between the two polymer systems were confirmed using Fourier transform infrared spectroscopy. The crosslinked polymers were porous, thus able to encapsulate bovine serum albumin (23 wt%) and then released the protein in a sustained fashion over 96 h. Concurrently, the hydrogel releases salicylic acid in a sustained manner up to 120 h. Hydrogel systems were cytocompatible at relevant therapeutic concentrations. These hydrogel systems can be used for simultaneous delivery of salicylic acid and protein to achieve synergic effects.

scholarly journals Synthetic nanoparticles of bovine serum albumin with entrapped salicylic acid

2016 ◽  
Vol Volume 10 ◽  
pp. 11-21 ◽  
Author(s):  
Erika Bronze-Uhle ◽  
Bruna Carolina Costa ◽  
Valdecir Farias Ximenes ◽  
Paulo Noronha Lisboa-Filho
Keyword(s):  
Salicylic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

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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