Optical rotation and anion binding in acid solutions of serum albumin
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Elsevier BV
Reference6 articles.
1. Conformation Changes in Bovine Plasma Albumin Associated with Hydrogen Ion and Urea Binding. I. Intrinsic Viscosity and Optical Rotation1,2
2. Optical rotation and viscosity of native and denatured proteins. I. Influence of pH, and the stability of various proteins toward several denaturing reagents
3. Changes in the Intrinsic Viscosity and Optical Rotation of Bovine Plasma Albumin Associated with Acid Binding1
4. Physical Chemistry of Protein Solutions. VII. The Binding of Some Small Anions to Serum Albumin1
5. Interaction of Homologous Alkyl Sulfates with Bovine Serum Albumin
Cited by 10 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Magnetic-Resonance Studies of the Interactions between Bovine-Serum Albumin and Surfactants. 2. Effect of Surfactants on the Structure of Bovine-Serum Albumin;European Journal of Biochemistry;1973-07
2. Konformationsinduzierter Circulardichroismus in Hamoglobinen von Chironomus th. thummi;European Journal of Biochemistry;1970-10
3. Binding of Organic Ions by Proteins;Multiple Equilibria in Proteins;1969
4. Mechanism of Protection by Anionic Detergents against Denaturation of Serum Albumin;Journal of Biological Chemistry;1964-11
5. Theoretische Grundlagen;Die Plasmaproteine in der Klinischen Medizin;1963
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