Sedimentation and optical rotation behavior of bovine plasma albumin at low pH in the presence of various anions. Effect of charge on molecular expansion
- 1 November 1957
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 72 (1) , 205-218
- https://doi.org/10.1016/0003-9861(57)90187-x
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Electrophoretic and Hydrogen Ion Binding Behavior of Bovine Plasma Albumin in the Presence of 0.02 M Thiocyanate IonJournal of the American Chemical Society, 1957
- Electrophoretic Behavior of Bovine Plasma Albumin At Low pHJournal of the American Chemical Society, 1957
- Physical Chemistry of Protein Solutions. VII. The Binding of Some Small Anions to Serum Albumin1Journal of the American Chemical Society, 1957
- POLYPEPTIDES. VII. POLY-γ-BENZYL-L-GLUTAMATE: THE HELIX-COIL TRANSITION IN SOLUTION1Journal of the American Chemical Society, 1956
- The Reversible Expansion of Bovine Serum Albumin in Acid Solutions1Journal of the American Chemical Society, 1955
- Thermodynamic Considerations of Protein Reactions.1,2 I. Modified Reactivity of Polar GroupsJournal of the American Chemical Society, 1954
- The Interaction of Optically Isomeric Dyes with Human Serum Albumin1Journal of the American Chemical Society, 1954
- Changes in the Intrinsic Viscosity and Optical Rotation of Bovine Plasma Albumin Associated with Acid Binding1Journal of the American Chemical Society, 1954
- Consideration of the Hydrodynamic Properties of Proteins1,2Journal of the American Chemical Society, 1953
- The Partial Specific Volumes, in Aqueous Solution, of Three ProteinsJournal of the American Chemical Society, 1952