Photoacids as a new fluorescence tool for tracking structural transitions of proteins: following the concentration-induced transition of bovine serum albumin

2015 ◽  
Vol 17 (47) ◽  
pp. 32023-32032 ◽  
Author(s):  
Nadav Amdursky

The concentration-induced structural transition of BSA at low pH was studied with photoacids. A special focus is also given to the discussion about the validity of other techniques to observe this transition.

1954 ◽  
Vol 32 (12) ◽  
pp. 1092-1099 ◽  
Author(s):  
M. E. Reichmann ◽  
P. A. Charlwood

Light-scattering measurements of bovine serum albumin made at pH 1.9 in 0.1 M-0.45 M potassium chloride show that the molecule is not dissociated, but has the same molecular weight as in neutral solution. At pH 1.9 in the absence of salt aggregation occurs, the extent increasing with time. The sedimentation constant at pH 1.9 increases from 3.2S in 0.1 M potassium chloride to 3.6 in the 0.5 M salt, compared with 4.3 in neutral solution. These differences are ascribed to changes of molecular shape.


Langmuir ◽  
2012 ◽  
Vol 28 (27) ◽  
pp. 10164-10176 ◽  
Author(s):  
Xiangyang Li ◽  
Yapeng Fang ◽  
Saphwan Al-Assaf ◽  
Glyn O. Phillips ◽  
Xiaolin Yao ◽  
...  

Biochemistry ◽  
1966 ◽  
Vol 5 (2) ◽  
pp. 684-689 ◽  
Author(s):  
Victor Bloomfield

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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