Protein—ligand interactions studied on bovine serum albumin with free and polymer-bound Cibacron Blue F3G-A as ligand with reference to affinity partitioning
- 31 December 1991
- journal article
- Published by Elsevier in Journal of Chromatography A
- Vol. 537, 219-233
- https://doi.org/10.1016/s0021-9673(01)88896-8
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Affinity partitioning: Development of mathematical model describing behavior of biomolecules in aqueous two‐phase systemsBiotechnology & Bioengineering, 1987
- Effect of polymer structure on affinity partitioning of lactate dehydrogenase in polymer—water two-phase systemsJournal of Chromatography A, 1987
- Partitioning in aqueous two-phase systems: An overviewAnalytical Biochemistry, 1986
- Aqueous two-phase systems in protein purificationJournal of Biotechnology, 1985
- Preparation of cibacron blue F3G‐A (polyethylene glycol) in large scale for use in affinity partitioningBiotechnology & Bioengineering, 1985
- Parameters determining affinity partitioning of yeast enzymes using polymer-bound triazine dye ligandsJournal of Chromatography A, 1984
- Dye-Ligand Affinity Chromatography: The Interaction of Cibacron Blue F3GA® with Proteins and EnzymeCritical Reviews in Biochemistry, 1984
- Comparison between binding analyses performed by equilibrium dialysis and partitioning in aqueous two-phase systems exemplified by the binding of cibacron blue to serum albuminJournal of Chromatography A, 1982
- Protein purification using immobilised triazine dyesJournal of Chromatography A, 1979
- Partition of trypsin in two‐phase systems containing a diamidino‐α, ω‐diphenylcarbamyl poly (ethylene glycol) as competitive inhibitor of trypsinFEBS Letters, 1974