Download Affinity Chromatography Methods and Protocols by Pascal Bailon PDF

By Pascal Bailon

Information strong affinity chromatography tools, starting from conventional affinity purification corresponding to immunoaffinity chromatography, to using the most recent phage-display expertise within the discovery of affinity ligands and medicine. additionally incorporated are separations of small molecules reminiscent of haptens, protein ligands, and supramolecular constructions. every one bankruptcy is dedicated to a selected approach and contains an advent, an evidence of rules, an in depth fabrics checklist, and directions. useful notes recommend replacement tactics and describe how one can triumph over difficulties. The editor works for an enormous pharmaceutical corporation.

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6. 7. 8. 9. 10. 51 Equilibrate the Protein A column with 5 column volumes (cv) of buffer A. Load supernatant onto Protein A column at 5 mL/min. Load up to 20 mg antibody/mL gel. Wash with 10 cv of buffer B. Elute antibody with 5 cv of buffer C. Re-equilibrate column with 2 cv of buffer A. Wash with 5 cv of buffer E followed by 10 cv of buffer A. The column is now ready for the next chromatography run. 3. Notes This general protocol works well with high-affinity antibodies and is independent of the particular Protein A gel used.

499, 235. 4. , and Olin, B. (1983) Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions. Biochemistry 22, 1621. 56 Schwarz 5. Hale, J. , and Beidler, D. E. (1994) Purification of humanized murine and murine monoclonal antibodies using immobilized metal-affinity chromatography. Anal. Biochem. 222, 29. 6. Al-Mashikhi, S. , and Nakai, S. (1988) Separation of immunoglobulins and lactoferrin from cheese whey by chelating chromatography.

1987) A survey of enzyme coupling techniques. Methods Enzymol. 135, 30–65. 3. , and Topper, Y. J. (1975) Structure of a soluble super-active insulin is revealed by the nature of the complex between cyanogen-bromide-activated Sepharose and amines. Proc. Nat. Acad. Sci. USA 72, 1055–1058. 4. Tesser, G. , Fisch, H. , and Schwyzer, R. (1974) Limitations of affinity chromatography: solvolytic detachment of ligands from polymeric supports. Helv. Chim. Acta. 57, 1718–1730. 5. Cuatrecasas, P. (1970) Protein purification by affinity chromatography.

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