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Affinity chromatography /
Bioaffinity chromatography has increasingly become the method of choice for the purification, determination or removal of many biologically active substances.
| Clasificación: | Libro Electrónico |
|---|---|
| Autor principal: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Amsterdam ; New York : New York :
Elsevier Scientific Pub. Co. ; Distributors for the U.S. and Canada, Elsevier North-Holland,
1978.
|
| Colección: | Journal of chromatography library ;
v. 12. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
Tabla de Contenidos:
- Front Cover; Affinity Chromatography; Copyright Page; Contents; Acknowledgements; Chapter 1. Introduction; References; Chapter 2. The principle history and use of affinity chromatography; References; Chapter 3. Theory of affiity chromatography; 3.1 Theoretical guidelines deduced on the basis of the equilibrium model; 3.2 Theory of cooperative bonding within the plate theory; 3.3 Statistical theory of chromatography applied to affinity chromatography; References; Chapter 4. Application of affinity chromatography to the quantitative evaluation of specific complexes
- 4.1 Determination of dissociation constants by elution analysis4.2 Determination of dissociation constants by frontal analysis; 4.3 Cooperative elution of oligoadenylic acid in immobilized polyuridylic acid chromatography; 4.4 Other methods for the quantitative evaluation of interactions with immobilized affinity ligands; References; Chapter 5. General considerations on affinant-sorbent bonding; 5.1 Steric accessibility; 5.2 Conformation of attached affinant; 5.3 Concentration of the affinant on the matrix; 5.4 Concentration of proteins equilibration time and flow-rate
- 5.5 Effect of temperature5.6 Effect of pH and ionic strength; 5.7 Elution with competitive affinity ligands; 5.8 Non-specific effects; References; Chapter 6. Choice of affinity ligands for attachment; 6.1 Highly specific and group-specific matrices; 6.2 Isolation of enzymes inhibitors and cofactors; 6.3 Immunoaffinity chromatography; 6.4 Isolation of lectins. glycoproteins and saccharides; 6.5 Isolation of receptors binding and transport protein; 6.6 Isolation of -SH proteins and peptides; 6.7 Isolation of specific peptides; 6.8 Isolation of nucleic acids and nucleotides
- 6.9 Isolation of lipids. hormones and other substances6.10 Isolation of cells and viruses; 6.11 Commercially available insoluble affinants; References; Chapter 7. Hydrophobic chromatography covalent affinity chromatography affinity elution and related methods; 7.1 Hydrophobic chromatography; 7.2 Covalent affinity chromatography; 7.3 Affinity elution; 7.4 Affinity density perturbation; 7.5 Affinity electrophoresis; 7.6 Metal chelate affinity chromatography; References; Chapter 8. Solid matrix supports and the most used methods of binding; 8.1 Required characteristics
- 8.2 Survey of the most common solid supports and coupling procedures8.3 Spacers; 8.4 Blocking of unreacted groups; 8.5 Leakage of the coupled affinant; 8.6 General considerations in the choice of sorbents, spacers and coupling and blocking procedures; References; Chapter 9. Characterization of supports and immobilized affinity ligands; 9.1 Methods for thedetermination of non-specific sorption; 9.2 Determination of activatable and active groups; 9.3 Methods for the determination of immobilized affinity ligands; 9.4 Active-site titration of immobilized proteases