The Binding of Indole Analogues to Defatted Human Serum Albumin at Different Chloride Concentrations
Open Access
- 1 September 1964
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 239 (9) , 2835-2841
- https://doi.org/10.1016/s0021-9258(18)93822-6
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Optical rotation and viscosity of native and denatured proteins. XII. Differences between human and bovine albuminsArchives of Biochemistry and Biophysics, 1958
- 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
- Physical Chemistry of Protein Solutions. VII. The Binding of Some Small Anions to Serum Albumin1Journal of the American Chemical Society, 1957
- Optical rotation and viscosity of native and denatured proteins. VI. Highly purified human serum albumin specimensArchives of Biochemistry and Biophysics, 1955
- The Reversible Expansion of Bovine Serum Albumin in Acid Solutions1Journal of the American Chemical Society, 1955
- Hydrogen Ion Equilibria of Bovine Serum Albumin1Journal of the American Chemical Society, 1955
- Changes in the Intrinsic Viscosity and Optical Rotation of Bovine Plasma Albumin Associated with Acid Binding1Journal of the American Chemical Society, 1954
- Phenolic Hydroxyl Ionization in Proteins. I. Bovine Serum Albumin1-3Journal of the American Chemical Society, 1952
- Preparation and Properties of Serum and Plasma Proteins. XXIII. Hydrogen Ion Equilibria in Native and Modified Human Serum Albumins1a, 1bJournal of the American Chemical Society, 1950
- Physical Chemistry of Protein Solutions. IV. The Combination of Human Serum Albumin with Chloride Ion1Journal of the American Chemical Society, 1950