The Kinetics of Protein Denaturation. III. The Optical Rotations of Serum Albumin, β-Lactoglobulin and Pepsin in Urea Solutions

1953 ◽  
Vol 75 (21) ◽  
pp. 5154-5157 ◽  
Author(s):  
W. Kauzmann ◽  
R. B. Simpson
Keyword(s):  
Serum Albumin ◽  
Protein Denaturation ◽  
Optical Rotations ◽  
Β Lactoglobulin ◽  
Kinetics Of

Kinetics of heat-induced whey protein denaturation and aggregation in skim milks with adjusted whey protein concentration

2005 ◽  
Vol 72 (3) ◽  
pp. 369-378 ◽  
Author(s):  
David J Oldfield ◽  
Harjinder Singh ◽  
Mike W Taylor
Keyword(s):  
Whey Protein ◽  
Protein Concentration ◽  
Protein Denaturation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Whey Proteins ◽  
Pilot Scale ◽  
Casein Micelles ◽  
Reaction Orders ◽  
Β Lactoglobulin ◽  
Kinetics Of

Microfiltration and ultrafiltration were used to manufacture skim milks with an increased or reduced concentration of whey proteins, while keeping the casein and milk salts concentrations constant. The skim milks were heated on a pilot-scale UHT plant at 80, 90 and 120 °C. The heat-induced denaturation and aggregation of β-lactoglobulin (β-lg), α-lactalbumin (α-la) and bovine serum albumin (BSA) were quantified by polyacrylamide gel electrophoresis. Apparent rate constants and reaction orders were calculated for β-lg, α-la and BSA denaturation. Rates of β-lg, α-la and BSA denaturation increased with increasing whey protein concentration. The rate of α-la and BSA denaturation was affected to a greater extent than β-lg by the change in whey protein concentration. After heating at 120 °C for 160 s, the concentration of β-lg and α-la associated with the casein micelles increased as the initial concentration of whey proteins increased.

Polarographic studies on renaturation of urea-denatured human serum albumin

1989 ◽  
Vol 54 (2) ◽  
pp. 536-543 ◽  
Author(s):  
Josef Chmelík ◽  
Pavel Anzenbacher ◽  
Vítěz Kalous
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Irreversible Process ◽  
State Model ◽  
Native Protein ◽  
Main Components ◽  
Two State Model ◽  
Kinetics Of

The renaturation of the two main components of human serum albumin, i.e. of mercaptalbumin and nonmercaptalbumin, was studied polarographically. It has been demonstrated that renaturation of both proteins after 1-min denaturation in 8M urea is reversible. By contrast, renaturation after 200 min denaturation in 8M urea is an irreversible process; the characteristics of renatured mercaptalbumin differ more from the properties of the native protein than the characteristics of nonmercaptalbumin. The studies of the kinetics of renaturation of both proteins have shown that the renaturation can be represented by a two-state model. This means that the existence of stable intermediary products during the renaturation process was not determined polarographically.

Stereoselective kinetics of warfarin binding to human serum albumin: Effect of an allosteric interaction

Chirality ◽  
2002 ◽  
Vol 14 (5) ◽  
pp. 442-448 ◽  
Author(s):  
Ilona Fitos ◽  
J�lia Visy ◽  
Julianna Kardos
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Allosteric Interaction ◽  
Kinetics Of
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