Polymer Resins with Amino Acid Containing Pendants for Sorption of Bilirubin. IV. Site Binding Constants
- 1 January 1989
- journal article
- research article
- Published by Taylor & Francis in Biomaterials, Artificial Cells and Artificial Organs
- Vol. 17 (2) , 137-151
- https://doi.org/10.3109/10731198909118275
Abstract
Site binding constants, calculated for the adsorption of bilirubin onto various lysine, arginine, or histidine containing oligopeptide-resins assuming either a one or two site binding model, are of the order of 104 M. Using these data it can be shown that there are positive cooperative effects for lysine-containing pendants, while arginine-containing pendants eventually result in negative cooperative behaviour. This difference in behaviour has been attributed to the difference in the side groups in the arginine and lysine pendants and is discussed in terms of the basicity of the amino acids, accessibility to the sites as a consequence of the flexibility or rigidity of the side group, and in terms of π-π electron interactions, where applicable.This publication has 13 references indexed in Scilit:
- A simplified analysis of scatchard plots for systems with two interacting binding sitesBiopolymers, 1988
- Immobilized replicates of sequence 136–148 of human serum albumin as adsorbents for bilirubinCanadian Journal of Chemistry, 1987
- Cooperative binding to macromolecules. A formal approachAccounts of Chemical Research, 1986
- Numbers of Receptor Sites from Scatchard Graphs: Facts and FantasiesScience, 1982
- Protein affinities for small molecules: Conceptions and misconceptionsArchives of Biochemistry and Biophysics, 1979
- Fragments of bovine serum albumin produced by limited proteolysis. Conformation and ligand bindingBiochemistry, 1975
- Properties of graphical representations of multiple classes of binding sitesBiochemistry, 1971