The salting-out behavior of bovine plasma albumin; further evidence for configurational isomerization
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference8 articles.
1. Conformation Changes in Bovine Plasma Albumin Associated with Hydrogen Ion and Urea Binding. II. Hydrogen Ion Titration Curves1,2
2. Proteins, Amino Acids, and Peptides;Cohn,1943
3. Changes in the Intrinsic Viscosity and Optical Rotation of Bovine Plasma Albumin Associated with Acid Binding1
4. The Reversible Expansion of Bovine Serum Albumin in Acid Solutions1
5. ELECTROPHORETIC DEMONSTRATION OF THE ISOMERIZATION OF BOVINE PLASMA ALBUMIN AT LOW pH
Cited by 16 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. Conformational changes of bovine plasma albumin prior to the salting-out of the protein in concentrated salt solution;International Journal of Peptide and Protein Research;2009-01-12
2. SOME ASPECTS OF THE STRUCTURE AND CONFORMATIONAL PROPERTIES OF SERUM ALBUMIN;Albumin: Structure, Function and Uses;1977
3. A new type of microheterogeneity of albumin from blood plasma;Bulletin of Experimental Biology and Medicine;1973-08
4. Reversible boundary spreading as a criterion of the microheterogeneity of plasma albumins;Biochemistry;1970-04-28
5. The Microheterogeneity of Plasma Albumins;Journal of Biological Chemistry;1965-10
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