Effect of pH on the ultrasonic absorption of aqueous solutions of proteins. Comments

1970 ◽  
Vol 74 (13) ◽  
pp. 2734-2736 ◽  
Author(s):  
Raoul Zana ◽  
Jacques Lang
Nature ◽  
1966 ◽  
Vol 210 (5038) ◽  
pp. 835-835 ◽  
Author(s):  
FABIO FITTIPALDI

2001 ◽  
Vol 229 (1-2) ◽  
pp. 57-66 ◽  
Author(s):  
Jonathan K. Armstrong ◽  
Babur Z. Chowdhry ◽  
Martin J. Snowden ◽  
Jingfeng Dong ◽  
Stephen A. Leharne

1962 ◽  
Vol 40 (3) ◽  
pp. 363-372 ◽  
Author(s):  
R. W. Burley ◽  
W. H. Cook

The effect of pH, temperature, ionic strength, and lipoprotein concentration on the reversible dissociation of α- and β-lipovitellin in aqueous solutions above pH 6 has been examined by ultracentrifugal measurements. Under otherwise similar conditions α- and β-lipovitellin are 50% dissociated at pH 10.5 and 7.8, respectively. Both lipovitellins undergo an irreversible aggregation above about pH 11; β-lipovitellin is sometimes converted to a non-dissociable form upon aging. Dissociation of both lipovitellins decreases with increasing ionic strength and increasing temperature. Although the ultracentrifugal method has limitations, provisional equilibrium constants and thermodynamic data were obtained from it that are comparable with those obtained for certain protein systems.


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