A Re-examination of the Acid Titration Behavior of Human Mercaptalbumin
Open Access
- 1 October 1962
- journal article
- Published by Elsevier
- Vol. 237 (10) , 3163-3170
- https://doi.org/10.1016/s0021-9258(18)50138-1
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- CoÖperative Transitions in the Binding of Hydrogen Ions by Plasma Albumin. A Proposed MechanismThe Journal of Physical Chemistry, 1957
- Theory of Protein Titration Curves. II. Calculations for Simple Models at Low Ionic StrengthJournal of the American Chemical Society, 1957
- Theory of Protein Titration Curves. I. General Equations for Impenetrable SpheresJournal 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
- Hydrodynamic and Thermodynamic Properties of Bovine Serum Albumin at Low pHThe Journal of Physical Chemistry, 1956
- ELECTROPHORETIC DEMONSTRATION OF THE ISOMERIZATION OF BOVINE PLASMA ALBUMIN AT LOW pHJournal of the American Chemical Society, 1956
- Bovine serum albumin and its behaviour in acid solutionBiochemical Journal, 1956
- The Reversible Expansion of Bovine Serum Albumin in Acid Solutions1Journal of the American Chemical Society, 1955
- The Electrostatic Free Energy of Globular Protein Ions in Aqueous Salt SolutionThe Journal of Physical Chemistry, 1955
- Changes in the Intrinsic Viscosity and Optical Rotation of Bovine Plasma Albumin Associated with Acid Binding1Journal of the American Chemical Society, 1954