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A synthetic ligand for IgA affinity purification

✍ Scribed by Giovanna Palombo; Sandro De Falco; Maria Tortora; Giovanni Cassani; Giorgio Fassina

Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
211 KB
Volume
11
Category
Article
ISSN
0952-3499

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✦ Synopsis

We reported previously that TG19318, a synthetic ligand deduced from the screening of combinatorial libraries, displays specific and selective recognition properties for immunoglobulins of the G class and can be used conveniently for affinity chromatography purification of monoclonal and polyclonal antibodies. In this study we have extended the ligand characterization, examining its ability to bind IgA from cell culture supernatants and from IgG-deprived serum. Affinity columns prepared by immobilizing TG19318 on Sepharose allowed convenient one-step purification of monoclonal IgA directly from crude feedstocks, in high yield and with full recovery of immunoreactivity. Optimal column adsorption occurred with phosphate buffer at neutral pH, while elution of adsorbed IgA could be accomplished by a buffer pH change to acidic or basic conditions. Column capacity was close to 7 mg IgA/ml support.

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