Temperature, pH and Additives Effects on the Binding of Caffeic Acid Phenethyl Ester to the Native State of Bovine Serum Albumin

Author(s):  
Xiao Nai ◽  
Yanrong Chen ◽  
Shengyu Hao ◽  
Min Liu ◽  
Qian Zhang ◽  
...  
1988 ◽  
Vol 13 (1) ◽  
pp. 11-14 ◽  
Author(s):  
T. Adzet ◽  
J. Camarasa ◽  
E. Escubedo ◽  
M. Merlos

2014 ◽  
Vol 145 ◽  
pp. 741-751 ◽  
Author(s):  
Atanu Singha Roy ◽  
Amit Kumar Dinda ◽  
Susmitnarayan Chaudhury ◽  
Swagata Dasgupta

Langmuir ◽  
2013 ◽  
Vol 30 (1) ◽  
pp. 278-287 ◽  
Author(s):  
Burcu Baykal Minsky ◽  
Bingqian Zheng ◽  
Paul L. Dubin

2017 ◽  
Vol 41 (24) ◽  
pp. 15003-15015 ◽  
Author(s):  
Aurica Precupas ◽  
Romica Sandu ◽  
Anca Ruxandra Leonties ◽  
Dan-Florin Anghel ◽  
Vlad Tudor Popa

Binding of caffeic acid at low concentrations to bovine serum albumin enhances the thermal stability of the protein.


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.


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