Quantitative affinity chromatography

Journal of Biochemical and Biophysical Methods

Volumn 49, Issue 1-3, 2001, Pages 99-121

  Winzor, Donald J ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Affinity chromatography; Biosensor technology; Ligand binding; Partition equilibrium; Solid phase immunoassays

Indexed keywords

CHEMICAL COMPOUND; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME; LACTATE DEHYDROGENASE; LIGAND;

AFFINITY CHROMATOGRAPHY; ARTICLE; BINDING AFFINITY; BIOSENSOR; CHEMICAL INTERACTION; COLUMN CHROMATOGRAPHY; CONCENTRATION (PARAMETERS); DATA ANALYSIS; EQUILIBRIUM CONSTANT; IMMUNOASSAY; MATHEMATICAL ANALYSIS; MUSCLE FIBRIL; PRIORITY JOURNAL; PROTEIN INTERACTION; PURIFICATION;

BIOSENSING TECHNIQUES; CHROMATOGRAPHY, AFFINITY; IMMUNOASSAY; INDICATORS AND REAGENTS; KINETICS; MATHEMATICS; PHARMACEUTICAL PREPARATIONS; SENSITIVITY AND SPECIFICITY;

EID: 0035975877     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-022X(01)00191-9     Document Type: Article

References (48)

1. Use of affinity chromatography for the quantitative study of acceptor-ligand interactions: The lactose synthetase system
2. Quantitative affinity chromatography: Determination of binding constants by elution with competitive inhibitors
3. Evaluation of equilibrium constants by affinity chromatography
4. Multivalency of the partitioning species in quantitative affinity chromatography: Evaluation of the site-binding constant for the aldolase-phosphate interaction from studies with cellulose phosphate as the affinity matrix
5. Equilibrium partition studies of the interaction between aldolase and myofibrils
6. Equilibrium partition studies of the myofibrillar interactions of glycolytic enzymes
7. Evaluation of equilibrium constants by solid-phase immunoassay: The binding of paraquat to its elicited mouse monoclonal antibody
8. Use of a biosensor with surface plasmon resonance detection for the determination of binding constants: Measurement of interleukin-6 binding to the soluble interleukin-6 receptor
9. Application of quantitative affinity chromatography to the study of protein-ligand interactions
10. Chromatographic study of the thermodynamic and kinetic characteristics of silica-bound Concanavalin A
11. Quantitative affinity chromatography: Further developments in the analysis of experimental results from column chromatographic and partition equilibrium experiments
12. Effects of ligand multivalency in binding studies: A general counterpart of the Scatchard analysis
13. Determination of binding constants by quantitative affinity chromatography: Current and future applications
14. The attraction of proteins for small molecules and ions
15. Studies of chemically reacting systems on Sephadex: 1. Chromatographic demonstration of the Gilbert theory
16. A quantitative study of biospecific desorption of rat liver (M4) lactate dehydrogenase from 10-carboxydecylamino-Sepharose: Determination of the number of ligand-binding sites blocked on adsorption
17. The application of the law of mass action to binding by proteins: Interactions with calcium
18. Molecular size distribution in three-dimensional polymers: 1. Gelation
19. The rectangular hyperbolic binding equation for multivalent ligands
20. Quantitative affinity chromatography: Increased versatility of the technique for studies of ligand binding
21. Zonal elution quantitative affinity chromatography and analysis of molecular interactions
22. Analytical affinity chromatography and characterization of biomolecular interactions
23. Quantitative analysis of affinity chromatography of trypsin: A new technique for investigation of protein-ligand interaction
24. Affinity chromatography of trypsin and related enzymes: V. Basic studies of quantitative affinity chromatography
25. Evaluation of equilibrium constants for the interaction of lactate dehydrogenase with reduced nicotinamide adenine dinucleotide
26. Use of quantitative affinity chromatography for characterizing high-affinity interactions: Binding of heparin to antithrombin III
27. Quantitative affinity chromatography
28. Measurement of binding constants by partition equilibrium methods
29. Thermodynamic characterization of the interactions of methotrexate with dihydrofolate reductase by quantitative affinity chromatography
30. The study of high-affinity interactions by quantitative affinity chromatography: Analytical expressions in terms of total ligand concentration
31. Evaluation of binding constants by frontal affinity chromatography
32. Immobilized membrane vesicle or proteosome affinity chromatography: Frontal analysis of interactions of cytochalasin B and d-glucose with the human red cell glucose transporter
33. Supramolecular organization of glycolytic enzymes
34. Graphical analysis of binding data reflecting competition between two ligands for the same acceptor sites
35. Enzyme kinetic evidence of active-site involvement in the interaction between aldolase and muscle myofibrils
36. Effect of calcium ion on the interaction of aldolase with rabbit muscle myofibrils
37. Metabolic dependence of glycolytic enzyme binding in rat and sheep heart
38. Further probes into quantitative aspects of competitive binding assays: Allowance for effects of antigen multivalency in immunoassays
39. Effects of solute multivalence on the evaluation of binding constants by biosensor technology studies with Concanavalin A and interleukin-6 as partitioning proteins
40. Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology
41. The resonant mirror: A novel optical biosensor for direct sensing of biomolecular interactions: 1. Principle of operation
42. Kinetic analysis of the mass transport limited interaction between the tyrosine kinase lck SH2 domain and a phosphorylated peptide studied by a new cuvette-based surface plasmon resonance instrument
43. Use of a resonant mirror biosensor to characterize the interaction of carboxypeptidase with an elicited monoclonal antibody
44. Determination of binding constants by equilibrium titration with a circulating sample in a surface plasmon resonance biosensor
45. Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins
46. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
47. Potential of biosensor technology for the characterization of interactions by quantitative affinity chromatography
48. From gel filtration to biosensor technology: The development of chromatography for the characterization of protein interactions