Structure-affinity relationship of the binding of phenolic acids and their derivatives to bovine serum albumin

2019 ◽  
Vol 278 ◽  
pp. 77-83 ◽  
Author(s):  
Sujing Yuan ◽  
Yunyue Zhang ◽  
Jiaxin Liu ◽  
Yu Zhao ◽  
Libo Tan ◽  
...  
2011 ◽  
Vol 44 (9) ◽  
pp. 2861-2867 ◽  
Author(s):  
Yuping Zhang ◽  
Shuyun Shi ◽  
Xiaorui Sun ◽  
Kelong Huang ◽  
Xiaoqin Chen ◽  
...  

Author(s):  
G. D. Gagne ◽  
M. F. Miller

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.


1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson

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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