On the Aggregation of Bovine Serum Albumin in 0.1 M Salt Solutions

1973 ◽  
Vol 51 (22) ◽  
pp. 3781-3788 ◽  
Author(s):  
Nanette O. Del Rosario ◽  
Siao Fang Sun

The molecular weight of bovine serum albumin at neutral pH in 0.1 M salt solutions was determined with light scattering measurements. Simultaneously, preferential binding of a salt to the protein was calculated. It was found that the protein aggregates in KI and KSCN, but not in KCl, LiCl, and LiBr solutions. Analysis of the sedimentation behavior has confirmed aggregation as a molecular phenomenon, not an artifact.

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.


1949 ◽  
Vol 27b (10) ◽  
pp. 791-806 ◽  
Author(s):  
H. J. Hadow ◽  
H. Sheffer ◽  
J. C. Hyde

Apparatus is described for the measurement of small amounts of scattered light, dissymmetry of radiation, depolarization, and very small refractive index differences. Methods of calibration are critically examined. Benzene was adopted as a turbidity standard. Measurements were made on fractionated polystyrene of known molecular weight and on bovine serum albumin solutions. Values of the reduced intensity for benzene were obtained:[Formula: see text]Degree and sources of error are discussed


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