Urea denaturation of bovine serum albumin at pH 9
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference26 articles.
1. The Kinetics of Protein Denaturation. III. The Optical Rotations of Serum Albumin, β-Lactoglobulin and Pepsin in Urea Solutions
2. The Kinetics of Protein Denaturation. V. The Viscosity of Urea Solutions of Serum Albumin1
3. The effect of disulfide bonding on the solubility of unfolded serum albumin in salt solutions
4. Sulfhydryl-Dependent Aggregation Accompanying the Denaturation of Bovine Plasma Albumin by Urea1,2
5. Dimerization of mercaptalbumin in presence of mercurials. III. Bovine mercaptalbumin in water and in concentrated urea solutions
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1. Adsorption of plasma proteins onto polymer latices;Advances in Colloid and Interface Science;1991-03
2. Different rates of formation of secondary and tertiary structure during renaturation of urea-denatured human serum albumin;Collection of Czechoslovak Chemical Communications;1989
3. Adsorption of heat-denatured albumin onto polymer latices;Journal of Colloid and Interface Science;1988-11
4. Thermal Denaturation and Coagulation of Whey Proteins: Effect of Sugars;Journal of Dairy Science;1988-01
5. Mechanism of denaturation of human serum albumin by urea;Collection of Czechoslovak Chemical Communications;1988
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