Performance of thiophilic adsorption chromatography in the purification of rat IgG2b monoclonal antibodies from serum- and protein-free culture supernatants

• Published in: Biomedical chromatography Vol. 13; no. 6; pp. 379 - 381
• Main Authors: Argüelles, María Eladia, Alonso, Marta, García Suárez, María del Mar, Barneo, Luis, Sampedro, Andrés, Toyos, Juan R. de los
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01-10-1999
• Subjects: Animals; Antibodies, Monoclonal - isolation & purification; Chromatography, Agarose - methods; Culture Media - chemistry; Hybridomas; Immunoglobulin G - isolation & purification; Proteins; Rats
• ISSN: 0269-3879; 1099-0801
• DOI: 10.1002/(SICI)1099-0801(199910)13:6<379::AID-BMC895>3.0.CO;2-X

The usefulness of thiophilic adsorption chromatography for the purification of rat IgG2b monoclonal antibodies has been evaluated. This approach has not shown specificity for immunoglobulins; therefore, to minimize potential interferences, the purification was carried out from supernatants of hybridomas grown in serum‐ and protein‐free conditions. The protein purity of the six final antibody preparations assayed was always ≥97%. In addition to the easiness of this procedure, which enables one‐step antibody purification, the materials employed are rather inexpensive and milligram amounts of antibody can be recovered from 1 L of supernatant. Overall, the purification of rat IgG2b monoclonals under the conditions reported here offers an advantageous alternative to other more expensive and cumbersome methods. Copyright © 1999 John Wiley & Sons, Ltd.