Hydrodynamic and Thermodynamic Properties of Bovine Serum Albumin at Low pH

1956 ◽  
Vol 60 (12) ◽  
pp. 1633-1644 ◽  
Author(s):  
George I. Loeb ◽  
Harold A. Scheraga
Keyword(s):  
Bovine Serum Albumin ◽  
Thermodynamic Properties ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Low Ph

Interactions between bovine serum albumin and sodium taurodeoxycholate: thermodynamic properties

2004 ◽  
Vol 418 (1-2) ◽  
pp. 69-77 ◽  
Author(s):  
Aida C. Palacios ◽  
Marta Letizia Antonelli ◽  
Camillo La Mesa
Keyword(s):  
Bovine Serum Albumin ◽  
Thermodynamic Properties ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sodium Taurodeoxycholate

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
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Structural Transition ◽  
Low Ph ◽  
Special Focus ◽  
Structural Transitions

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.

LIGHT-SCATTERING AND SEDIMENTATION STUDIES OF BOVINE SERUM ALBUMIN AT LOW pH

1954 ◽  
Vol 32 (12) ◽  
pp. 1092-1099 ◽  
Author(s):  
M. E. Reichmann ◽  
P. A. Charlwood
Keyword(s):  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Potassium Chloride ◽  
Bovine Serum ◽  
Molecular Shape ◽  
Low Ph ◽  
Neutral Solution ◽  
Sedimentation Constant ◽  
Scattering Measurements

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.

The Structure of Bovine Serum Albumin at Low pH*

Biochemistry ◽  
1966 ◽  
Vol 5 (2) ◽  
pp. 684-689 ◽  
Author(s):  
Victor Bloomfield
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Low Ph

Thermodynamic properties of the bovine serum albumin–sodium taurodeoxycholate system

2004 ◽  
Vol 246 (1-3) ◽  
pp. 127-134 ◽  
Author(s):  
Marta L. Antonelli ◽  
Antonio Capalbi ◽  
Giacomo Gente ◽  
Aida C. Palacios ◽  
Simona Sallustio ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Thermodynamic Properties ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sodium Taurodeoxycholate

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.

Sign in / Sign up

Export Citation Format

Share Document