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Journal article
Quantitative Affinity Chromatography. Determination of Binding Constants by Elution with Competitive Inhibitors
Proceedings of the National Academy of Sciences - PNAS, v 71(6), pp 2382-2385
01 Jun 1974
PMID: 4526212
Abstract
The affinity chromatographic separation procedure was tested for its utility in quantitating the affinity of proteins to both insolubilized ligand and corresponding competing soluble ligand. An expression has been derived that (
1
) allows the determination of binding constants for the interaction of a soluble protein species with an affinity chromatography matrix involving active site binding, (
2
) yields binding constants for the interaction of the protein with soluble ligands that can compete with the insoluble matrix for binding to the active site of the protein, and (
3
) utilizes readily obtainable parameters from conventional chromatography. This expression has been applied to the quantitation of the binding of staphylococcal nuclease to thymidine-5′-phosphate-3′-amino-phenylphosphate-Sepharose in competition with thymidine-3′,5′-bisphosphate.
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Details
- Title
- Quantitative Affinity Chromatography. Determination of Binding Constants by Elution with Competitive Inhibitors
- Creators
- Ben M. Dunn - National Institutes of HealthIrwin M. Chaiken - National Institutes of Health
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 71(6), pp 2382-2385
- Publisher
- PNAS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; Drexel University
- Web of Science ID
- WOS:A1974T571900051
- Scopus ID
- 2-s2.0-0000469640
- Other Identifier
- 991019520714804721