Key result
Affinity chromatographic methods for purifying antibodies involve various matrices, attachment chemistries, and ligands to optimize product yield and minimize denaturation.
This review provides a comprehensive overview of affinity chromatographic methods for antibody purification.
Answers are grounded in this paper and cite their sources.
May guide lab optimization of antibody purification; leaves open standardization for clinical-grade use.
Affinity chromatographic methods for purifying antibodies are reviewed. Topics reviewed include (a) the matrices used in the preparation of the affinity supports; (b) the chemistries commonly used to attach affinity ligands directly on hydroxyl‐carrying supports and indirectly through the use of bifunctional agents to crosslink the affinity ligands to the supports; (c) methods for detecting ligand leakage; (d) macromolecular affinity ligands; (e) low molecular weight peptidyl affinity ligands; (f) low molecular weight non‐peptidyl affinity ligands; (g) optimal conditions for achieving improved product yield; and (h) optimal elution systems that minimize the denaturation of the purified antibodies.
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Ngo et al. (2007) conducted a review in Antibody purification. Affinity chromatographic methods was evaluated. Affinity chromatographic methods for purifying antibodies involve various matrices, attachment chemistries, and ligands to optimize product yield and minimize denaturation.
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